메뉴 건너뛰기




Volumn 16, Issue 7, 2011, Pages 3072-3132

Light-induced water oxidation in photosystem II

Author keywords

Electron transfer; ENDOR; EPR; FTIR; Proton transfer; Review; X ray crystallography; X ray spectroscopy

Indexed keywords

ALGAE; CYANOBACTERIA;

EID: 79959542061     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3900     Document Type: Article
Times cited : (33)

References (493)
  • 2
    • 57849127933 scopus 로고    scopus 로고
    • Primary Processes of Photosynthesis - Principles and Apparatus
    • Ed D. P. Häder and G. Jori. RSC Publishing, Cambridge
    • G. Renger: Primary Processes of Photosynthesis - Principles and Apparatus. In: Comprehensive Series in Photochemistry and Photobiology. Ed D. P. Häder and G. Jori. RSC Publishing, Cambridge (2008)
    • (2008) Comprehensive Series in Photochemistry and Photobiology
    • Renger, G.1
  • 3
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobaoterial photosystem I at 2.5 A resolution
    • DOI 10.1038/35082000
    • P. Jordan, P. Fromme, H. T. Witt, O. Klukas, W. Saenger and N. Krauss: Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411, 909-917 (2001) (Pubitemid 32601481)
    • (2001) Nature , vol.411 , Issue.6840 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 4
    • 34247576821 scopus 로고    scopus 로고
    • The structure of a plant photosystem I supercomplex at 3.4 A resolution
    • DOI 10.1038/nature05687, PII NATURE05687
    • A. Amunts, O. Drory and N. Nelson: The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature 447, 58-63 (2007) (Pubitemid 46685832)
    • (2007) Nature , vol.447 , Issue.7140 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 5
    • 77449145132 scopus 로고    scopus 로고
    • Structure Determination and Improved Model of Plant Photosystem i
    • A. Amunts, H. Toporik, A. Borovikova and N. Nelson: Structure Determination and Improved Model of Plant Photosystem I. J Biol Chem 285, 3478-3486 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 3478-3486
    • Amunts, A.1    Toporik, H.2    Borovikova, A.3    Nelson, N.4
  • 6
    • 0242494128 scopus 로고    scopus 로고
    • 6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
    • DOI 10.1126/science.1090165
    • G. Kurisu, H. Zhang, J. L. Smith and W. A. Cramer: Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302, 1009-1014 (2003) (Pubitemid 37386186)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 7
    • 0344497439 scopus 로고    scopus 로고
    • 6f complex
    • DOI 10.1038/nature02155
    • D. Stroebel, Y. Choquet, J. L. Popot and D. Picot: An atypical haem in the cytochrome b6f complex. Nature 426, 413-418 (2003) (Pubitemid 37490123)
    • (2003) Nature , vol.426 , Issue.6965 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.-L.3    Picot, D.4
  • 8
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • DOI 10.1038/nature02373
    • Z. Liu, H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An and W. Chang: Crystal structure of spinach major lightharvesting complex at 2.72 Å resolution. Nature 428, 287-292 (2004) (Pubitemid 38418793)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 9
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution
    • DOI 10.1038/sj.emboj.7600585
    • J. Standfuss, A. C. Terwisscha van Scheltinga, M. Lamborghini and W. Kühlbrandt: Mechanisms of photoprotection and nonphotochemical quenching in pea lightharvesting complex at 2.5 Å resolution. EMBO J 24, 919-928 (2005) (Pubitemid 40470141)
    • (2005) EMBO Journal , vol.24 , Issue.5 , pp. 919-928
    • Standfuss, J.1    Van Scheltinga, A.C.T.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 10
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 A resolution
    • DOI 10.1038/35055589
    • A. Zouni, H. T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger and P. Orth: Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739-743 (2001) (Pubitemid 32144521)
    • (2001) Nature , vol.409 , Issue.6821 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 12
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the Photosynthetic Oxygen-Evolving Center
    • DOI 10.1126/science.1093087
    • K. N. Ferreira, T. M. Iverson, K. Maghlaoui, J. Barber and S. Iwata: Architecture of the photosynthetic oxygen-evolving center. Science 303, 1831-1838 (2004) (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 13
    • 8144227878 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.2 Å resolution: A closer look at the Mn-cluster
    • J. Biesiadka, B. Loll, J. Kern, K. D. Irrgang and A. Zouni: Crystal structure of cyanobacterial photosystem II at 3.2 Å resolution: a closer look at the Mn-cluster. Phys Chem Chem Phys 6, 4733-4736 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4733-4736
    • Biesiadka, J.1    Loll, B.2    Kern, J.3    Irrgang, K.D.4    Zouni, A.5
  • 14
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • DOI 10.1038/nature04224, PII NATURE04224
    • B. Loll, J. Kern, W. Saenger, A. Zouni and J. Biesiadka: Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438, 1040-1044 (2005) (Pubitemid 43093979)
    • (2005) Nature , vol.438 , Issue.7070 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 15
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9 Å resolution: Role of quinones, lipids, channels and chloride
    • A. Guskov, J. Kern, A. Gabdulkhakov, M. Broser, A. Zouni and W. Saenger: Cyanobacterial photosystem II at 2.9 Å resolution: role of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16, 334-342 (2009)
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5    Saenger, W.6
  • 16
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • D. M. Rees, A. G. W. Leslie and J. E. Walker: The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci U S A 106, 21597-21601 (2009)
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.W.2    Walker, J.E.3
  • 17
    • 70349828967 scopus 로고    scopus 로고
    • High-resolution structure of the rotor ring of a protondependent ATP synthase
    • D. Pogoryelov, O. Yildiz, J. D. Faraldo-Gomez and T. Meier: High-resolution structure of the rotor ring of a protondependent ATP synthase. Nat Struct Mol Biol 16, 1068-1073 (2009)
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1068-1073
    • Pogoryelov, D.1    Yildiz, O.2    Faraldo-Gomez, J.D.3    Meier, T.4
  • 19
    • 45749150851 scopus 로고    scopus 로고
    • Photosystem II: The lightdriven water:plastoquinone oxidoreductase
    • Ed Govindjee. Springer, Dordrecht
    • T. Wydrzynski and K. Satoh: Photosystem II: the lightdriven water:plastoquinone oxidoreductase. In: Advances in Photosynthesis and Respiration. Ed Govindjee. Springer, Dordrecht (2005)
    • (2005) Advances in Photosynthesis and Respiration
    • Wydrzynski, T.1    Satoh, K.2
  • 20
    • 36849071982 scopus 로고    scopus 로고
    • Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase
    • DOI 10.1007/s11120-007-9201-1, Govindjee Special Issue: Part B, Celebrating Govindjee's 50 Years in Photosynthesis Research and his 75th Birthday
    • J. Kern and G. Renger: Photosystem II: structure and mechanism of the water:plastoquinone oxidoreductase. Photosynth Res 94, 183-202 (2007) (Pubitemid 350229101)
    • (2007) Photosynthesis Research , vol.94 , Issue.2-3 , pp. 183-202
    • Kern, J.1    Renger, G.2
  • 21
    • 57849146011 scopus 로고    scopus 로고
    • Photosystem II: The machinery of photosynthetic water splitting
    • DOI 10.1007/s11120-008-9345-7
    • G. Renger and T. Renger: Photosystem II: The machinery of photosynthetic water splitting. Photosynth Res 98, 53-80 (2008) (Pubitemid 50289510)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 53-80
    • Renger, G.1    Renger, T.2
  • 23
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem II
    • DOI 10.1021/cr0204294
    • J. P. McEvoy and G. W. Brudvig: Water-splitting chemistry of photosystem II. Chem Rev 106, 4455-4483 (2006) (Pubitemid 44816649)
    • (2006) Chemical Reviews , vol.106 , Issue.11 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 24
    • 34547851705 scopus 로고    scopus 로고
    • 4-Ca cluster as derived from X-ray diffraction
    • DOI 10.1007/s11120-007-9173-1, Photosynthetic Water Oxidation
    • J. Kern, J. Biesiadka, B. Loll, W. Saenger and A. Zouni: Structure of the Mn4-Ca cluster as derived from X-ray diffraction. Photosynth Res 92, 389-405 (2007) (Pubitemid 47246541)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 389-405
    • Kern, J.1    Biesiadka, J.2    Loll, B.3    Saenger, W.4    Zouni, A.5
  • 25
    • 38049016877 scopus 로고    scopus 로고
    • The manganese complex of photosystem II in its reaction cycle - Basic framework and possible realization at the atomic level
    • H. Dau and M. Haumann: The manganese complex of photosystem II in its reaction cycle - Basic framework and possible realization at the atomic level. Coord Chem Rev 252, 273-295 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 273-295
    • Dau, H.1    Haumann, M.2
  • 26
    • 38049082074 scopus 로고    scopus 로고
    • Revealing the structure of the Mn-cluster of photosystem II by X-ray crystallography
    • J. Barber and J. W. Murray: Revealing the structure of the Mn-cluster of photosystem II by X-ray crystallography. Coord Chem Rev 252, 233-243 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 233-243
    • Barber, J.1    Murray, J.W.2
  • 27
    • 57849103639 scopus 로고    scopus 로고
    • From cell growth to the 3.0 Å resolution crystal structure of cyanobacterial photosystem II
    • Ed G. Renger. RSC Publishing, Cambridge
    • A. Zouni: From Cell Growth to the 3.0 Å Resolution Crystal Structure of Cyanobacterial Photosystem II. In: Primary Processes of Photosynthesis, Principles and Apparatus. Ed G. Renger. RSC Publishing, Cambridge, 2, 193-236 (2008)
    • (2008) Primary Processes of Photosynthesis, Principles and Apparatus , vol.2 , pp. 193-236
    • Zouni, A.1
  • 28
    • 77956220438 scopus 로고    scopus 로고
    • Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6-Å resolution
    • M. Broser, A. Gabdulkhakov, J. Kern, A. Guskov, F. Müh, W. Saenger and A. Zouni: Crystal Structure of Monomeric Photosystem II from Thermosynechococcus elongatus at 3.6-Å Resolution. J Biol Chem 285, 26255-26262 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 26255-26262
    • Broser, M.1    Gabdulkhakov, A.2    Kern, J.3    Guskov, A.4    Müh, F.5    Saenger, W.6    Zouni, A.7
  • 30
    • 40849139152 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.0 Å resolution: A closer look at the antenna system and the small membrane-intrinsic subunits
    • F. Müh, T. Renger and A. Zouni: Crystal structure of cyanobacterial photosystem II at 3.0 Å resolution: a closer look at the antenna system and the small membrane-intrinsic subunits. Plant Physiol Biochem 46, 238-264 (2008)
    • (2008) Plant Physiol Biochem , vol.46 , pp. 238-264
    • Müh, F.1    Renger, T.2    Zouni, A.3
  • 31
    • 1042290470 scopus 로고    scopus 로고
    • The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
    • DOI 10.1016/j.bbabio.2003.12.004
    • L. X. Shi and W. P. Schröder: The low molecular mass subunits of the photosynthetic supracomplex, photosystem II. Biochim Biophys Acta 1608, 75-96 (2004) (Pubitemid 38198252)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1608 , Issue.2-3 , pp. 75-96
    • Shi, L.-X.1    Schroder, W.P.2
  • 34
    • 34547839673 scopus 로고    scopus 로고
    • The extrinsic proteins of Photosystem II
    • DOI 10.1007/s11120-006-9117-1, Photosynthetic Water Oxidation
    • J. L. Roose, K. M. Wegener and H. B. Pakrasi: The extrinsic proteins of Photosystem II. Photosynth Res 92, 369-387 (2007) (Pubitemid 47246537)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 369-387
    • Roose, J.L.1    Wegener, K.M.2    Pakrasi, H.B.3
  • 35
    • 57849142823 scopus 로고    scopus 로고
    • Structures and functions of the extrinsic proteins of photosystem II from different species
    • DOI 10.1007/s11120-008-9343-9
    • I. Enami, A. Okumura, R. Nagao, T. Suzuki, M. Iwai and J. R. Shen: Structures and functions of the extrinsic proteins of photosystem II from different species. Photosynth Res 98, 349-363 (2008) (Pubitemid 50247998)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 349-363
    • Enami, I.1    Okumura, A.2    Nagao, R.3    Suzuki, T.4    Iwai, M.5    Shen, J.-R.6
  • 36
    • 38049011376 scopus 로고    scopus 로고
    • Primary photochemistry and energetics leading to the oxidation of the (Mn)4Ca cluster and to the evolution of molecular oxygen in Photosystem II
    • F. Rappaport and B. A. Diner: Primary photochemistry and energetics leading to the oxidation of the (Mn)4Ca cluster and to the evolution of molecular oxygen in Photosystem II. Coord Chem Rev 252, 259-272 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 37
    • 77951191914 scopus 로고    scopus 로고
    • Primary photophysical processes in photosystem II: Bridging the gap between crystal structure and optical spectra
    • T. Renger and E. Schlodder: Primary Photophysical Processes in Photosystem II: Bridging the Gap between Crystal Structure and Optical Spectra. ChemPhysChem 11, 1141-1153 (2010)
    • (2010) ChemPhysChem , vol.11 , pp. 1141-1153
    • Renger, T.1    Schlodder, E.2
  • 38
    • 57849118283 scopus 로고    scopus 로고
    • Primary light-energy conversion in tetrameric chlorophyll structure of photosystem II and bacterial reaction centers: I. A review
    • DOI 10.1007/s11120-008-9370-6
    • R. A. Khatypov, A. Y. Khmelnitskiy, M. M. Leonova, L. G. Vasilieva and V. A. Shuvalov: Primary light-energy conversion in tetrameric chlorophyll structure of photosystem II and bacterial reaction centers: I. A review. Photosynth Res 98, 81-93 (2008) (Pubitemid 50300662)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 81-93
    • Khatypov, R.A.1    Khmelnitskiy, A.Yu.2    Leonova, M.M.3    Vasilieva, L.G.4    Shuvalov, V.A.5
  • 39
    • 0242709278 scopus 로고    scopus 로고
    • Light-harvesting antennas in photosynthesis
    • Ed Govindjee. Springer (Kluwer Academic Publishers), Dordrecht, The Netherlands
    • B. R. Green and W. W. Parson: Light-Harvesting Antennas in Photosynthesis. In: Advances in Phothosynthesis and Respiration. Ed Govindjee. Springer (Kluwer Academic Publishers), Dordrecht, The Netherlands (2003)
    • (2003) Advances in Phothosynthesis and Respiration
    • Green, B.R.1    Parson, W.W.2
  • 40
    • 56349090168 scopus 로고    scopus 로고
    • Structure and function of photosystem II light-harvesting proteins (Lhcb) of higher plants
    • Ed G. Renger. RSC Publishing, Cambridge, U. K.
    • H. van Amerongen and R. Croce: Structure and Function of Photosystem II Light-Harvesting Proteins (Lhcb) of Higher Plants. In: Primary Processes of Photosynthesis, Principles and Apparatus. Ed G. Renger. RSC Publishing, Cambridge, U. K., 1, 329-367 (2008)
    • (2008) Primary Processes of Photosynthesis, Principles and Apparatus , vol.1 , pp. 329-367
    • Van Amerongen, H.1    Croce, R.2
  • 41
    • 41549127157 scopus 로고    scopus 로고
    • Light harvesting in photosystem II core complexes is limited by the transfer to the trap: Can the core complex turn into a photoprotective mode?
    • DOI 10.1021/ja7099826
    • G. Raszewski and T. Renger: Light harvesting in photosystem II core complexes is limited by the transfer to the trap: Can the core complex turn into a photoprotective mode? J Am Chem Soc 130, 4431-4446 (2008) (Pubitemid 351466439)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.13 , pp. 4431-4446
    • Raszewski, G.1    Renger, T.2
  • 42
    • 33144465946 scopus 로고    scopus 로고
    • Charge separation kinetics in intact photosystem II core particles is trap-limited. A picosecond fluorescence study
    • DOI 10.1021/bi052248c
    • Y. Miloslavina, M. Szczepaniak, M. G. Müller, J. Sander, M. Nowaczyk, M. Rögner and A. R. Holzwarth: Charge separation kinetics in intact photosystem II core particles is trap-limited. A picosecond fluorescence study. Biochemistry 45, 2436-2442 (2006) (Pubitemid 43271344)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2436-2442
    • Miloslavina, Y.1    Szczepaniak, M.2    Muller, M.G.3    Sander, J.4    Nowaczyk, M.5    Rogner, M.6    Holzwarth, A.R.7
  • 43
    • 52949142767 scopus 로고    scopus 로고
    • Fluorescence lifetime spectrum of the plant photosystem II core complex: Photochemistry does not induce specific reaction center quenching
    • G. Tumino, A. P. Casazza, E. Engelmann, F. M. Garlaschi, G. Zucchelli and R. C. Jennings: Fluorescence lifetime spectrum of the plant photosystem II core complex: photochemistry does not induce specific reaction center quenching. Biochemistry 47, 10449-10457 (2008)
    • (2008) Biochemistry , vol.47 , pp. 10449-10457
    • Tumino, G.1    Casazza, A.P.2    Engelmann, E.3    Garlaschi, F.M.4    Zucchelli, G.5    Jennings, R.C.6
  • 44
    • 8144230860 scopus 로고    scopus 로고
    • On the role of the CP47 core antenna in the energy transfer and trapping dynamics of Photosystem II
    • E. G. Andrizhiyevskaya, D. Frolov, R. van Grondelle and J. P. Dekker: On the role of the CP47 core antenna in the energy transfer and trapping dynamics of Photosystem II. Phys Chem Chem Phys 6, 4810-4819 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4810-4819
    • Andrizhiyevskaya, E.G.1    Frolov, D.2    Van Grondelle, R.3    Dekker, J.P.4
  • 45
    • 0024433591 scopus 로고
    • The photosynthetic reaction center from this purple bacterium Rhodopseudomonas viridis
    • J. Deisenhofer and H. Michel: The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis. Science 245, 1463-1473 (1989) (Pubitemid 19243235)
    • (1989) Science , vol.245 , Issue.4925 , pp. 1463-1473
    • Deisenhofer, J.1    Michel, H.2
  • 46
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • DOI 10.1126/science.276.5313.812
    • M. H. B. Stowell, T. M. McPhillips, D. C. Rees, S. M. Soltis, E. Abresch and G. Feher: Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer. Science 276, 812-816 (1997) (Pubitemid 27199864)
    • (1997) Science , vol.276 , Issue.5313 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 47
    • 34447282051 scopus 로고    scopus 로고
    • pH Modulates the Quinone Position in the Photosynthetic Reaction Center from Rhodobacter sphaeroides in the Neutral and Charge Separated States
    • DOI 10.1016/j.jmb.2007.04.082, PII S0022283607005311
    • J. Koepke, E. M. Krammer, A. R. Klingen, P. Sebban, G. M. Ullmann and G. Fritzsch: pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states. J Mol Biol 371, 396-409 (2007) (Pubitemid 47048266)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 396-409
    • Koepke, J.1    Krammer, E.-M.2    Klingen, A.R.3    Sebban, P.4    Ullmann, G.M.5    Fritzsch, G.6
  • 48
    • 57849153635 scopus 로고    scopus 로고
    • Structure of reaction centers in anoxygenic bacteria
    • Ed G. Renger. RSC Publishing, Cambridge
    • C. R. D. Lancaster: Structure of Reaction Centers in Anoxygenic Bacteria. In: Primary Processes of Photosynthesis, Principles and Apparatus. Ed G. Renger. RSC Publishing, Cambridge, 2, 5-56 (2008)
    • (2008) Primary Processes of Photosynthesis, Principles and Apparatus , vol.2 , pp. 5-56
    • Lancaster, C.R.D.1
  • 49
    • 0014101751 scopus 로고
    • A 2nd chlorophyll reaction in electron chain of photosynthesis - Registration by repetitive excitation technique
    • G. Döring, H. H. Stiehl and H. T. Witt: A 2nd Chlorophyll Reaction in Electron Chain of Photosynthesis - Registration by Repetitive Excitation Technique. Z Naturforsch B 22, 639-644 (1967)
    • (1967) Z Naturforsch B , vol.22 , pp. 639-644
    • Döring, G.1    Stiehl, H.H.2    Witt, H.T.3
  • 51
    • 40549136513 scopus 로고    scopus 로고
    • Spectroscopic properties of reaction center pigments in photosystem II core complexes: Revision of the multimer model
    • G. Raszewski, B. A. Diner, E. Schlodder and T. Renger: Spectroscopic properties of reaction center pigments in photosystem II core complexes: revision of the multimer model. Biophys J 95, 105-119 (2008)
    • (2008) Biophys J , vol.95 , pp. 105-119
    • Raszewski, G.1    Diner, B.A.2    Schlodder, E.3    Renger, T.4
  • 52
    • 18744387983 scopus 로고    scopus 로고
    • The first picoseconds in bacterial photosynthesis - Ultrafast electron transfer for the efficient conversion of light energy
    • DOI 10.1002/cphc.200400458
    • W. Zinth and J. Wachtveitl: The first picoseconds in bacterial photosynthesis - Ultrafast electron transfer for the efficient conversion of light energy. ChemPhysChem 6, 871-880 (2005) (Pubitemid 40669550)
    • (2005) ChemPhysChem , vol.6 , Issue.5 , pp. 871-880
    • Zinth, W.1    Wachtveitl, J.2
  • 53
    • 0037188022 scopus 로고    scopus 로고
    • Pigment-protein interactions in bacterial reaction centers and their influence on oxidation potential and spin density distribution of the primary donor
    • DOI 10.1021/jp0131119
    • F. Müh, F. Lendzian, M. Roy, J. C. Williams, J. P. Allen and W. Lubitz: Pigment-protein interactions in bacterial reaction centers and their influence on oxidation potential and spin density distribution of the primary donor. J Phys Chem B 106, 3226-3236 (2002) (Pubitemid 35290275)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.12 , pp. 3226-3236
    • Muh, F.1    Lendzian, F.2    Roy, M.3    Williams, J.C.4    Allen, J.P.5    Lubitz, W.6
  • 54
    • 1842555190 scopus 로고    scopus 로고
    • A Unified Description of the Electrochemical, Charge Distribution, and Spectroscopic Properties of the Special-Pair Radical Cation in Bacterial Photosynthesis
    • DOI 10.1021/ja036883m
    • J. R. Reimers and N. S. Hush: Unified description of the electrochemical, charge distribution, and spectroscopic properties of the special-pair radical cation in bacterial photosynthesis. J Am Chem Soc 126, 4132-4144 (2004) (Pubitemid 38453873)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.13 , pp. 4132-4144
    • Reimers, J.R.1    Hush, N.S.2
  • 55
    • 33845281185 scopus 로고
    • Spectroscopic properties of photosynthetic reaction centers .1. Theory
    • A. Warshel and W. W. Parson: Spectroscopic Properties of Photosynthetic Reaction Centers .1. Theory. J Am Chem Soc 109, 6143-6152 (1987)
    • (1987) J Am Chem Soc , vol.109 , pp. 6143-6152
    • Warshel, A.1    Parson, W.W.2
  • 56
    • 70349156478 scopus 로고    scopus 로고
    • Deciphering the influence of short-range electronic couplings on optical properties of molecular dimers: Application to "special pairs" in photosynthesis
    • M. E. Madjet, F. Müh and T. Renger: Deciphering the influence of short-range electronic couplings on optical properties of molecular dimers: application to "special pairs" in photosynthesis. J Phys Chem B 113, 12603-12614 (2009)
    • (2009) J Phys Chem B , vol.113 , pp. 12603-12614
    • Madjet, M.E.1    Müh, F.2    Renger, T.3
  • 58
    • 77949381093 scopus 로고    scopus 로고
    • Structure-based calculations of optical spectra of photosystem i suggest an asymmetric light-harvesting process
    • J. Adolphs, F. Müh, M. E. A. Madjet, M. Schmidt am Busch and T. Renger: Structure-Based Calculations of Optical Spectra of Photosystem I Suggest an Asymmetric Light-Harvesting Process. J Am Chem Soc 132, 3331-3343 (2010)
    • (2010) J Am Chem Soc , vol.132 , pp. 3331-3343
    • Adolphs, J.1    Müh, F.2    Madjet, M.E.A.3    Schmidt Am Busch, M.4    Renger, T.5
  • 60
    • 0030921067 scopus 로고    scopus 로고
    • A new pathway for transmembrane electron transfer in photosynthetic reaction centers of Rhodobacter sphaeroides not involving the excited special pair
    • DOI 10.1021/bi9703756
    • M. E. van Brederode, M. R. Jones, F. van Mourik, I. H. M. van Stokkum and R. van Grondelle: A new pathway for transmembrane electron transfer in photosynthetic reaction centers of Rhodobacter sphaeroides not involving the excited special pair. Biochemistry 36, 6855-6861 (1997) (Pubitemid 27258097)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 6855-6861
    • Van Brederode, M.E.1    Jones, M.R.2    Van Mourik, F.3    Van Stokkum, I.H.M.4    Van Grondelle, R.5
  • 61
    • 67749137704 scopus 로고    scopus 로고
    • Protein dynamics-induced variation of excitation energy transfer pathways
    • M. Brecht, V. Radics, J. B. Nieder and R. Bittl: Protein dynamics-induced variation of excitation energy transfer pathways. Proc Natl Acad Sci U S A 106, 11857-11861 (2009)
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11857-11861
    • Brecht, M.1    Radics, V.2    Nieder, J.B.3    Bittl, R.4
  • 62
    • 67749106269 scopus 로고    scopus 로고
    • Spectroscopic characterization of photosystem i at the single-molecule level
    • M. Brecht: Spectroscopic characterization of photosystem I at the single-molecule level. Mol Phys 107, 1955-1974 (2009)
    • (2009) Mol Phys , vol.107 , pp. 1955-1974
    • Brecht, M.1
  • 63
    • 34548210433 scopus 로고    scopus 로고
    • Mixing of exciton and charge-transfer states in photosystem II reaction centers: Modeling of stark spectra with modified redfield theory
    • DOI 10.1529/biophysj.106.096867
    • V. I. Novoderezhkin, J. P. Dekker and R. van Grondelle: Mixing of exciton and charge-transfer states in Photosystem II reaction centers: Modeling of stark spectra with modified Redfield theory. Biophys J 93, 1293-1311 (2007) (Pubitemid 47330909)
    • (2007) Biophysical Journal , vol.93 , Issue.4 , pp. 1293-1311
    • Novoderezhkin, V.I.1    Dekker, J.P.2    Van Grondelley, R.3
  • 65
    • 0242474251 scopus 로고
    • Enhancement in chlorella
    • J. Myers and J. R. Graham: Enhancement in Chlorella. Plant Physiol 38, 105-116 (1963)
    • (1963) Plant Physiol , vol.38 , pp. 105-116
    • Myers, J.1    Graham, J.R.2
  • 66
    • 0025973559 scopus 로고
    • Effect of irradiance level on distribution of chlorophylls between PS II and PS i as determined from optical cross-sections
    • N. L. Greenbaum and D. Mauzerall: Effect of Irradiance Level on Distribution of Chlorophylls between PS II and PS I as Determined from Optical Cross-Sections. Biochim Biophys Acta 1057, 195-207 (1991)
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 195-207
    • Greenbaum, N.L.1    Mauzerall, D.2
  • 67
    • 21744440606 scopus 로고    scopus 로고
    • The longwavelength limit of plant photosynthesis
    • H. Pettai, V. Oja, A. Freiberg and A. Laisk: The longwavelength limit of plant photosynthesis. FEBS Lett 579, 4017-4019 (2005)
    • (2005) FEBS Lett , vol.579 , pp. 4017-4019
    • Pettai, H.1    Oja, V.2    Freiberg, A.3    Laisk, A.4
  • 68
    • 21744451946 scopus 로고    scopus 로고
    • Photosynthetic activity of far-red light in green plants
    • DOI 10.1016/j.bbabio.2005.05.005, PII S0005272805001192
    • H. Pettai, V. Oja, A. Freiberg and A. Laisk: Photosynthetic activity of far-red light in green plants. Biochim Biophys Acta 1708, 311-321 (2005) (Pubitemid 40943595)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.3 , pp. 311-321
    • Pettai, H.1    Oja, V.2    Freiberg, A.3    Laisk, A.4
  • 69
    • 25444508945 scopus 로고    scopus 로고
    • Oxygen-evolving Photosystem II core complexes: A new paradigm based on the spectral identification of the charge-separating state, the primary acceptor and assignment of low-temperature fluorescence
    • DOI 10.1039/b417905f
    • E. Krausz, J. L. Hughes, P. Smith, R. Pace and S. P. Arskold: Oxygen-evolving Photosystem II core complexes: a new paradigm based on the spectral identification of the charge-separating state, the primary acceptor and assignment of low-temperature fluorescence. Photochem Photobiol Sci 4, 744-753 (2005) (Pubitemid 41367027)
    • (2005) Photochemical and Photobiological Sciences , vol.4 , Issue.9 , pp. 744-753
    • Krausz, E.1    Hughes, J.L.2    Smith, P.3    Pace, R.4    Arskold, S.P.5
  • 70
    • 33746576099 scopus 로고    scopus 로고
    • Charge separation in photosystem II core complexes induced by 690-730 nm excitation at 1.7K
    • DOI 10.1016/j.bbabio.2006.05.035, PII S0005272806001721
    • J. L. Hughes, P. Smith, R. Pace and E. Krausz: Charge separation in photosystem II core complexes induced by 690-730 nm excitation at 1.7 K. Biochim Biophys Acta 1757, 841-851 (2006) (Pubitemid 44142424)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.7 , pp. 841-851
    • Hughes, J.L.1    Smith, P.2    Pace, R.3    Krausz, E.4
  • 72
    • 34249780832 scopus 로고    scopus 로고
    • Steady-state and transient polarized absorption spectroscopy of photosytem I complexes from the cyanobacteria Arthrospira platensis and Thermosynechococcus elongatus
    • DOI 10.1016/j.bbabio.2007.01.013, PII S0005272807000175, Structure and Function of Photosystems
    • E. Schlodder, V. V. Shubin, E. El-Mohsnawy, M. Roegner and N. V. Karapetyan: Steady-state and transient polarized absorption spectroscopy of photosytem complexes from the cyanobacteria Arthrospira platensis and Thermosynechococcus elongatus. Biochim Biophys Acta 1767, 732-741 (2007) (Pubitemid 46855743)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 732-741
    • Schlodder, E.1    Shubin, V.V.2    El-Mohsnawy, E.3    Roegner, M.4    Karapetyan, N.V.5
  • 73
    • 0042368510 scopus 로고    scopus 로고
    • Two distinct conformations of the primary electron donor in reaction centers from Rhodobacter sphaeroides revealed by ENDOR/TRIPLE-spectroscopy
    • DOI 10.1021/bi962859s
    • F. Müh, J. Rautter and W. Lubitz: Two distinct conformations of the primary electron donor in reaction centers from Rhodobacter sphaeroides revealed by ENDOR/TRIPLE-spectroscopy. Biochemistry 36, 4155-4162 (1997) (Pubitemid 27171587)
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4155-4162
    • Muh, F.1    Rautter, J.2    Lubitz, W.3
  • 76
    • 0242657390 scopus 로고    scopus 로고
    • Proton transfer pathways and mechanism in bacterial reaction centers
    • DOI 10.1016/S0014-5793(03)01149-9
    • M. L. Paddock, G. Feher and M. Y. Okamura: Proton transfer pathways and mechanism in bacterial reaction centers. FEBS Lett 555, 45-50 (2003) (Pubitemid 37431095)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 77
    • 52949129815 scopus 로고    scopus 로고
    • Coupling of electron transfer to proton uptake at the QB site of the bacterial reaction center: A perspective from FTIR difference spectroscopy
    • E. Nabedryk and J. Breton: Coupling of electron transfer to proton uptake at the QB site of the bacterial reaction center: A perspective from FTIR difference spectroscopy. Biochim Biophys Acta 1777, 1229-1248 (2008)
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1229-1248
    • Nabedryk, E.1    Breton, J.2
  • 78
    • 33751242792 scopus 로고    scopus 로고
    • Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules
    • DOI 10.1021/bi060742q
    • S. Hermes, J. M. Stachnik, D. Onidas, A. Remy, E. Hofmann and K. Gerwert: Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules. Biochemistry 45, 13741-13749 (2006) (Pubitemid 44788744)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13741-13749
    • Hermes, S.1    Stachnik, J.M.2    Onidas, D.3    Remy, A.4    Hofmann, E.5    Gerwert, K.6
  • 80
    • 64349113842 scopus 로고    scopus 로고
    • Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from rhodobacter sphaeroides
    • T. Iwata, M. L. Paddock, M. Y. Okamura and H. Kandori: Identification of FTIR Bands Due to Internal Water Molecules around the Quinone Binding Sites in the Reaction Center from Rhodobacter sphaeroides. Biochemistry 48, 1220-1229 (2009)
    • (2009) Biochemistry , vol.48 , pp. 1220-1229
    • Iwata, T.1    Paddock, M.L.2    Okamura, M.Y.3    Kandori, H.4
  • 81
    • 34447576871 scopus 로고    scopus 로고
    • ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (QB- *) in reaction centers from Rhodobacter sphaeroides
    • DOI 10.1021/bi7005256
    • M. L. Paddock, M. Flores, R. Isaacson, C. Chang, E. C. Abresch and M. Y. Okamura: ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (QB -*) in reaction centers from Rhodobacter sphaeroides. Biochemistry 46, 8234-8243 (2007) (Pubitemid 47075963)
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8234-8243
    • Paddock, M.L.1    Flores, M.2    Isaacson, R.3    Chang, C.4    Abresch, E.C.5    Okamura, M.Y.6
  • 82
    • 3042687860 scopus 로고    scopus 로고
    • B redox state in reaction centers from Rhodobacter sphaeroides
    • DOI 10.1021/ja038092q
    • H. Ishikita and E. W. Knapp: Variation of Ser-L223 hydrogen bonding with the QB redox state in reaction centers from Rhodobacter sphaeroides. J Am Chem Soc 126, 8059-8064 (2004) (Pubitemid 38812797)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.25 , pp. 8059-8064
    • Ishikita, H.1    Knapp, E.-W.2
  • 83
    • 27144512716 scopus 로고    scopus 로고
    • Control of quinone redox potentials in Photosystem II: Electron transfer and photoprotection
    • DOI 10.1021/ja052567r
    • H. Ishikita and E. W. Knapp: Control of quinone redox potentials in photosystem II: Electron transfer and photoprotection. J Am Chem Soc 127, 14714-14720 (2005) (Pubitemid 41511009)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.42 , pp. 14714-14720
    • Ishikita, H.1    Knapp, E.-W.2
  • 84
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • DOI 10.1038/nsb954
    • A. Remy and K. Gerwert: Coupling of light-induced electron transfer to proton uptake in photosynthesis. Nat Struct Biol 10, 637-644 (2003) (Pubitemid 36944717)
    • (2003) Nature Structural Biology , vol.10 , Issue.8 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 86
    • 34247254284 scopus 로고    scopus 로고
    • B in Rhodobacter sphaeroides reaction centers provide evidence against the presence of a proposed transient electron acceptor X between the two quinones
    • DOI 10.1021/bi700297b
    • J. Breton: Steady-state FTIR spectra of the photoreduction of QA and QB in Rhodobacter sphaeroides reaction centers provide evidence against the presence of a proposed transient electron acceptor X between the two quinones. Biochemistry 46, 4459-4465 (2007) (Pubitemid 46625505)
    • (2007) Biochemistry , vol.46 , Issue.15 , pp. 4459-4465
    • Breton, J.1
  • 87
    • 35549006301 scopus 로고    scopus 로고
    • Redox potential of the non-heme iron complex in bacterial photosynthetic reaction center
    • DOI 10.1016/j.bbabio.2007.08.004, PII S0005272807001788
    • H. Ishikita, A. Galstyan and E. W. Knapp: Redox potential of the non-heme iron complex in bacterial photosynthetic reaction center. Biochim Biophys Acta 1767, 1300-1309 (2007) (Pubitemid 350007426)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.11 , pp. 1300-1309
    • Ishikita, H.1    Galstyan, A.2    Knapp, E.-W.3
  • 88
    • 0001700716 scopus 로고
    • Identification of Q400, a high-potential electron-acceptor of photosystem II, with the iron of the quinone-iron acceptor complex
    • V. Petrouleas and B. A. Diner: Identification of Q400, a High-Potential Electron-Acceptor of Photosystem II, with the Iron of the Quinone-Iron Acceptor Complex. Biochim Biophys Acta 849, 264-275 (1986)
    • (1986) Biochim Biophys Acta , vol.849 , pp. 264-275
    • Petrouleas, V.1    Diner, B.A.2
  • 89
    • 0029584591 scopus 로고
    • 13C-labeled bicarbonate
    • DOI 10.1021/bi00050a008
    • R. Hienerwadel and C. Berthomieu: Bicarbonate binding to the non-heme iron of photosystem II investigated by Fourier transform infrared difference spectroscopy and 13C-labeled bicarbonate. Biochemistry 34, 16288-16297 (1995) (Pubitemid 26006471)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16288-16297
    • Hienerwadel, R.1    Berthomieu, C.2
  • 90
    • 0001578731 scopus 로고
    • Photosystem II reaction center and bicarbonate
    • Ed J. Deisenhofer and J. R. Norris. Academic Press, Orlando
    • Govindjee and J. J. S. van Rensen: Photosystem II Reaction Center and Bicarbonate. In: The Photosynthetic Reaction Center Ed J. Deisenhofer and J. R. Norris. Academic Press, Orlando, 1, 357-389 (1993)
    • (1993) The Photosynthetic Reaction Center , vol.1 , pp. 357-389
    • Govindjee1    Van Rensen, J.J.S.2
  • 91
    • 0032926394 scopus 로고    scopus 로고
    • Role of bicarbonate in photosystem II, the water-plastoquinone oxido-reductase of plant photosynthesis
    • J. J. S. van Rensen, C. H. Xu and Govindjee: Role of bicarbonate in photosystem II, the water-plastoquinone oxido-reductase of plant photosynthesis. Physiol Plant 105, 585-592 (1999)
    • (1999) Physiol Plant , vol.105 , pp. 585-592
    • Van Rensen, J.J.S.1    Xu, C.H.2    Govindjee3
  • 92
    • 70349928560 scopus 로고    scopus 로고
    • The semiquinone-iron complex of photosystem II: Structural insights from ESR and theoretical simulation; Evidence that the native ligand to the non-heme iron is carbonate
    • N. Cox, L. Jin, A. Jaszewski, P. J. Smith, E. Krausz, A. W. Rutherford and R. Pace: The semiquinone-iron complex of photosystem II: structural insights from ESR and theoretical simulation; evidence that the native ligand to the non-heme iron is carbonate. Biophys J 97, 2024-2033 (2009)
    • (2009) Biophys J , vol.97 , pp. 2024-2033
    • Cox, N.1    Jin, L.2    Jaszewski, A.3    Smith, P.J.4    Krausz, E.5    Rutherford, A.W.6    Pace, R.7
  • 93
    • 0035799313 scopus 로고    scopus 로고
    • B pocket studied by fourier transform infrared spectroscopy
    • DOI 10.1021/bi002236l
    • C. Berthomieu and R. Hienerwadel: Iron coordination in photosystem II: interaction between bicarbonate and the QB pocket studied by Fourier transform infrared spectroscopy. Biochemistry 40, 4044-4052 (2001) (Pubitemid 32280442)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 4044-4052
    • Berthomieu, C.1    Hienerwadel, R.2
  • 94
    • 34848863975 scopus 로고    scopus 로고
    • The thylakoid proton motive force in vivo. Quantitative, non-invasive probes, energetics, and regulatory consequences of light-induced pmf
    • DOI 10.1016/j.bbabio.2007.07.006, PII S0005272807001557
    • K. Takizawa, J. A. Cruz, A. Kanazawa and D. M. Kramer: The thylakoid proton motive force in vivo. Quantitative, non-invasive probes, energetics, and regulatory consequences of light-induced pmf. Biochim. Biophys. Acta 1767, 1233-44 (2007) (Pubitemid 47498308)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1233-1244
    • Takizawa, K.1    Cruz, J.A.2    Kanazawa, A.3    Kramer, D.M.4
  • 96
    • 0002514628 scopus 로고
    • Electrochemistry of chlorophylls
    • Ed H. Scheer. CRC Press, Boca Raton
    • T. Watanabe and M. Kobayashi: Electrochemistry of chlorophylls. In: Chlorophylls. Ed H. Scheer. CRC Press, Boca Raton, 287-315 (1991)
    • (1991) Chlorophylls , pp. 287-315
    • Watanabe, T.1    Kobayashi, M.2
  • 98
    • 84980182243 scopus 로고
    • A new model of photochemical centers in system II
    • P. Joliot, G. Barbieri and R. Chabaud: A New Model of Photochemical Centers in System II. Photochem Photobiol 10, 309-329 (1969)
    • (1969) Photochem Photobiol , vol.10 , pp. 309-329
    • Joliot, P.1    Barbieri, G.2    Chabaud, R.3
  • 100
    • 84981598890 scopus 로고
    • 2 evolution - II. Damping of flash yield oscillation, deactivation
    • 2 Evolution - II. Damping of Flash Yield Oscillation, Deactivation. Photochem Photobiol 14, 307-321 (1971)
    • (1971) Photochem Photobiol , vol.14 , pp. 307-321
    • Forbush, B.1    Kok, B.2    McGloin, M.P.3
  • 101
    • 0025946303 scopus 로고
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids. Biochemistry 30, 7852-7862 (1991)
    • (1991) Biochemistry , vol.30 , pp. 7852-7862
    • Messinger, J.1    Wacker, U.2    Renger, G.3
  • 102
    • 0001105468 scopus 로고    scopus 로고
    • Molecular mechanism of water oxidation
    • Ed G. S. Singhal, G. Renger, Govindjee, K. D. Irrgang and S. K. Sopory. Kluwer Academic Publisher (now Springer) and Narosa Publishing, Dordrecht, Delhi
    • G. Renger: Molecular mechanism of water oxidation. In: Concepts in photobiology: photosynthesis and photomorphogenesis. Ed G. S. Singhal, G. Renger, Govindjee, K. D. Irrgang and S. K. Sopory. Kluwer Academic Publisher (now Springer) and Narosa Publishing, Dordrecht, Delhi, 292-329 (1999)
    • (1999) Concepts in Photobiology: Photosynthesis and Photomorphogenesis , pp. 292-329
    • Renger, G.1
  • 103
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • B. A. Barry and G. T. Babcock: Tyrosine radicals are involved in the photosynthetic oxygen-evolving system. Proc Natl Acad Sci U S A 84, 7099-7103 (1987)
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 104
    • 11244276886 scopus 로고    scopus 로고
    • Flash-induced oxygen evolution in photosynthesis: Simple solution for the extended S-state model that includes misses, double-hits, inactivation, and backward-transitions
    • DOI 10.1529/biophysj.104.050898
    • V. P. Shinkarev: Flash-induced oxygen evolution in photosynthesis: simple solution for the extended S-state model that includes misses, double-hits, inactivation, and backward-transitions. Biophys. J 88, 412-421 (2005) (Pubitemid 40070687)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 412-421
    • Shinkarev, V.P.1
  • 105
    • 84981610773 scopus 로고
    • Studies of system II photocenters by comparative measurements of luminescence, fluorescence, and oxygen emission
    • P. Joliot, A. Joliot, B. Bouges and G. Barbieri: Studies of System II Photocenters by Comparative Measurements of Luminescence, Fluorescence, and Oxygen Emission. Photochem Photobiol 14, 287-305 (1971)
    • (1971) Photochem Photobiol , vol.14 , pp. 287-305
    • Joliot, P.1    Joliot, A.2    Bouges, B.3    Barbieri, G.4
  • 106
    • 0015914834 scopus 로고
    • Limiting steps in photosystem II and water decomposition in chlorella and spinach chloroplasts
    • B. Bouges-Bocquet: Limiting Steps in Photosystem II and Water Decomposition in Chlorella and Spinach Chloroplasts. Biochim Biophys Acta 292, 772-785 (1973)
    • (1973) Biochim Biophys Acta , vol.292 , pp. 772-785
    • Bouges-Bocquet, B.1
  • 107
    • 0016698580 scopus 로고
    • The reactivation of epr signal ii in chloroplasts treated with reduced dichlorophenol-indophenol: Evidence against a dark equilibrium between two oxidation-states of the oxygen evolving system
    • B. R. Velthuys and J. W. M. Visser: The Reactivation of EPR Signal II in Chloroplasts Treated with Reduced Dichlorophenol-Indophenol: Evidence against a Dark Equilibrium between Two Oxidation-States of the Oxygen Evolving System. FEBS Lett 55, 109-112 (1975)
    • (1975) FEBS Lett , vol.55 , pp. 109-112
    • Velthuys, B.R.1    Visser, J.W.M.2
  • 108
    • 0000119587 scopus 로고
    • The reduction of the oxygen-evolving system in chloroplasts by thylakoid components
    • W. F. J. Vermaas, G. Renger and G. Dohnt: The Reduction of the Oxygen-Evolving System in Chloroplasts by Thylakoid Components. Biochim Biophys Acta 764, 194-202 (1984)
    • (1984) Biochim Biophys Acta , vol.764 , pp. 194-202
    • Vermaas, W.F.J.1    Renger, G.2    Dohnt, G.3
  • 111
    • 34249847311 scopus 로고    scopus 로고
    • Eight steps preceding O-O bond formation in oxygenic photosynthesis-A basic reaction cycle of the Photosystem II manganese complex
    • DOI 10.1016/j.bbabio.2007.02.022, PII S0005272807000631, Structure and Function of Photosystems
    • H. Dau and M. Haumann: Eight steps preceding O-O bond formation in oxygenic photosynthesis - a basic reaction cycle of the Photosystem II manganese complex. Biochim Biophys Acta 1767, 472-483 (2007) (Pubitemid 46860310)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 472-483
    • Dau, H.1    Haumann, M.2
  • 113
    • 0029956768 scopus 로고    scopus 로고
    • Binary oscillations in the Kok model of oxygen evolution in oxygenic photosynthesis
    • V. P. Shinkarev: Binary oscillations in the Kok model of oxygen evolution in oxygenic photosynthesis. Photosynth Res 48, 411-417 (1996) (Pubitemid 26367857)
    • (1996) Photosynthesis Research , vol.48 , Issue.3 , pp. 411-417
    • Shinkarev, V.P.1
  • 114
    • 0038650623 scopus 로고    scopus 로고
    • Oxygen evolution in photosynthesis: Simple analytical solution for the Kok model
    • V. P. Shinkarev: Oxygen evolution in photosynthesis: simple analytical solution for the Kok model. Biophys J 85, 435-441 (2003) (Pubitemid 36753647)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 435-441
    • Shinkarev, V.P.1
  • 115
    • 76149085834 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy
    • J. Yano and V. K. Yachandra: X-ray absorption spectroscopy. Photosynth Res 102, 241-254 (2009)
    • (2009) Photosynth Res , vol.102 , pp. 241-254
    • Yano, J.1    Yachandra, V.K.2
  • 116
    • 76149118072 scopus 로고    scopus 로고
    • X-ray emission spectroscopy
    • U. Bergmann and P. Glatzel: X-ray emission spectroscopy. Photosynth Res 102, 255-266 (2009)
    • (2009) Photosynth Res , vol.102 , pp. 255-266
    • Bergmann, U.1    Glatzel, P.2
  • 117
    • 38049016880 scopus 로고    scopus 로고
    • X-ray spectroscopy of the photosynthetic oxygen-evolving complex
    • K. Sauer, J. Yano and V. K. Yachandra: X-ray spectroscopy of the photosynthetic oxygen-evolving complex. Coord Chem Rev 252, 318-335 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 318-335
    • Sauer, K.1    Yano, J.2    Yachandra, V.K.3
  • 118
    • 0035999847 scopus 로고    scopus 로고
    • Radicals, radical pairs and triplet states in photosynthesis
    • W. Lubitz, F. Lendzian and R. Bittl: Radicals, radical pairs and triplet states in photosynthesis. Acc Chem Res 35, 313-320 (2002)
    • (2002) Acc Chem Res , vol.35 , pp. 313-320
    • Lubitz, W.1    Lendzian, F.2    Bittl, R.3
  • 119
    • 34547830285 scopus 로고    scopus 로고
    • EPR spectroscopy of the manganese cluster of photosystem II
    • DOI 10.1007/s11120-007-9194-9, Photosynthetic Water Oxidation
    • A. Haddy: EPR spectroscopy of the manganese cluster of photosystem II. Photosynth Res 92, 357-368 (2007) (Pubitemid 47246543)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 357-368
    • Haddy, A.1
  • 120
    • 76149132330 scopus 로고    scopus 로고
    • Electron-nuclear double resonance
    • L. Kulik and W. Lubitz: Electron-nuclear double resonance. Photosynth Res 102, 391-401 (2009)
    • (2009) Photosynth Res , vol.102 , pp. 391-401
    • Kulik, L.1    Lubitz, W.2
  • 121
    • 0016957826 scopus 로고
    • Observation and interpretation of X-Ray absorption edges in iron compounds and proteins
    • R. G. Shulman, Y. Yafet, P. Eisenberger and W. E. Blumberg: Observation and Interpretation of X-Ray Absorption Edges in Iron Compounds and Proteins. Proc Natl Acad Sci U S A 73, 1384-1388 (1976)
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 1384-1388
    • Shulman, R.G.1    Yafet, Y.2    Eisenberger, P.3    Blumberg, W.E.4
  • 122
    • 0001206702 scopus 로고
    • The state of manganese in the photosynthetic apparatus .3. Light-induced-changes in X-Ray Absorption (K-Edge) energies of manganese in photosynthetic membranes
    • D. B. Goodin, V. K. Yachandra, R. D. Britt, K. Sauer and M. P. Klein: The State of Manganese in the Photosynthetic Apparatus .3. Light-Induced-Changes in X-Ray Absorption (K-Edge) Energies of Manganese in Photosynthetic Membranes. Biochim Biophys Acta 767, 209-216 (1984)
    • (1984) Biochim Biophys Acta , vol.767 , pp. 209-216
    • Goodin, D.B.1    Yachandra, V.K.2    Britt, R.D.3    Sauer, K.4    Klein, M.P.5
  • 125
    • 0026685787 scopus 로고
    • X-ray detection of the period-four cycling of the manganese cluster in photosynthetic water oxidizing enzyme
    • T. A. Ono, T. Noguchi, Y. Inoue, M. Kusunoki, T. Matsushita and H. Oyanagi: X-ray Detection of the Period-Four Cycling of the Manganese Cluster in Photosynthetic Water Oxidizing Enzyme. Science 258, 1335-1337 (1992) (Pubitemid 23007782)
    • (1992) Science , vol.258 , Issue.5086 , pp. 1335-1337
    • Ono, T.1    Noguchi, T.2    Inoue, Y.3    Kusunoki, M.4    Matsushita, T.5    Oyanagi, H.6
  • 128
    • 0141780871 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy to analyze nuclear geometry and electronic structure of biological metal centers-potential and questions examined with special focus on the tetra-nuclear manganese complex of oxygenic photosynthesis
    • DOI 10.1007/s00216-003-1982-2
    • H. Dau, P. Liebisch and M. Haumann: X-ray absorption spectroscopy to analyze nuclear geometry and electronic structure of biological metal centers-potential and questions examined with special focus on the tetranuclear manganese complex of oxygenic photosynthesis. Anal Bioanal Chem 376, 562-583 (2003) (Pubitemid 40882966)
    • (2003) Analytical and Bioanalytical Chemistry , vol.376 , Issue.5 , pp. 562-583
    • Dau, H.1    Liebisch, P.2    Haumann, M.3
  • 129
    • 0000583959 scopus 로고
    • Manganese K-edge X-ray-absorption spectra of the cyclic S-states in the photosynthetic oxygen-evolving system
    • M. Kusunoki, T. Ono, T. Noguchi, Y. Inoue and H. Oyanagi: Manganese K-Edge X-Ray-Absorption Spectra of the Cyclic S-States in the Photosynthetic Oxygen-Evolving System. Photosynth Res 38, 331-339 (1993)
    • (1993) Photosynth Res , vol.38 , pp. 331-339
    • Kusunoki, M.1    Ono, T.2    Noguchi, T.3    Inoue, Y.4    Oyanagi, H.5
  • 130
    • 0027173103 scopus 로고
    • Where plants make oxygen: A structural model for the photosynthetic oxygen-evolving manganese cluster
    • V. K. Yachandra, V. J. DeRose, M. J. Latimer, I. Mukerji, K. Sauer and M. P. Klein: Where Plants Make Oxygen - a Structural Model for the Photosynthetic Oxygen-Evolving Manganese Cluster. Science 260, 675-679 (1993) (Pubitemid 23167590)
    • (1993) Science , vol.260 , Issue.5108 , pp. 675-679
    • Yachandra, V.K.1    DeRose, V.J.2    Latimer, M.J.3    Mukerji, I.4    Sauer, K.5    Klein, M.P.6
  • 135
    • 0026502537 scopus 로고
    • 2-evolving complex
    • A. Haddy, W. R. Dunham, R. H. Sands and R. Aasa: Multifrequency EPR Investigations into the Origin of the S2-State Signal at g = 4 of the O2-Evolving Complex. Biochim Biophys Acta 1099, 25-34 (1992)
    • (1992) Biochim Biophys Acta , vol.1099 , pp. 25-34
    • Haddy, A.1    Dunham, W.R.2    Sands, R.H.3    Aasa, R.4
  • 136
    • 0028986529 scopus 로고
    • 2 state multiline electron paramagnetic resonance signal of photosystem II: A multifrequency approach
    • K. A. Ahrling and R. J. Pace: Simulation of the S2 State Multiline Electron Paramagnetic Resonance Signal of Photosystem II: A Multifrequency Approach. Biophys J 68, 2081-2090 (1995)
    • (1995) Biophys J , vol.68 , pp. 2081-2090
    • Ahrling, K.A.1    Pace, R.J.2
  • 137
    • 0001339888 scopus 로고    scopus 로고
    • Multifrequency high-field EPR study of the interaction between the tyrosyl Z radical and the manganese cluster in plant photosystem II
    • P. Dorlet, A. Boussac, A. W. Rutherford and S. Un: Multifrequency high-field EPR study of the interaction between the tyrosyl Z radical and the manganese cluster in plant photosystem II. J Phys Chem B 103, 10945-10954 (1999)
    • (1999) J Phys Chem B , vol.103 , pp. 10945-10954
    • Dorlet, P.1    Boussac, A.2    Rutherford, A.W.3    Un, S.4
  • 138
    • 0001090546 scopus 로고
    • Intermediates of a polynuclear manganese center involved in photosynthetic oxidation of water
    • G. C. Dismukes and Y. Siderer: Intermediates of a Polynuclear Manganese Center Involved in Photosynthetic Oxidation of Water. Proc Natl Acad Sci U S A 78, 274-278 (1981)
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 274-278
    • Dismukes, G.C.1    Siderer, Y.2
  • 139
    • 0001849969 scopus 로고
    • EPR studies of the oxygen-evolving enzyme of photosystem II
    • J. L. Zimmermann and A. W. Rutherford: EPR Studies of the Oxygen-Evolving Enzyme of Photosystem II. Biochim Biophys Acta 767, 160-167 (1984)
    • (1984) Biochim Biophys Acta , vol.767 , pp. 160-167
    • Zimmermann, J.L.1    Rutherford, A.W.2
  • 140
    • 85022449453 scopus 로고
    • The origin of the multiline and g = 4.1 electron-paramagnetic resonance signals from the oxygen-evolving system of photosystem II
    • Ö. Hansson, R. Aasa and T. Vänngard: The Origin of the Multiline and g = 4.1 Electron-Paramagnetic Resonance Signals from the Oxygen-Evolving System of Photosystem II. Biophys J 51, 825-832 (1987)
    • (1987) Biophys J , vol.51 , pp. 825-832
    • Hansson, O.1    Aasa, R.2    Vänngard, T.3
  • 141
    • 33746328682 scopus 로고    scopus 로고
    • 2-state manganese cluster in single crystals of cyanobacterial photosystem II studied by W-band electron paramagnetic resonance spectroscopy
    • DOI 10.1021/jp055008f
    • 2-state manganese cluster in single crystals of cyanobacterial photosystem II studied by W-band electron paramagnetic resonance spectroscopy. J Phys Chem B 110, 13242-13247 (2006) (Pubitemid 44115662)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.26 , pp. 13242-13247
    • Matsuoka, H.1    Furukawa, K.2    Kato, T.3    Mino, H.4    Shen, J.-R.5    Kawamori, A.6
  • 142
    • 33745142521 scopus 로고    scopus 로고
    • 2 multiline signal of photosystem II
    • DOI 10.1016/j.febslet.2006.05.039, PII S0014579306006399
    • 2 multiline signal of Photosystem II. FEBS Lett 580, 3605-3609 (2006) (Pubitemid 43902794)
    • (2006) FEBS Letters , vol.580 , Issue.15 , pp. 3605-3609
    • Teutloff, C.1    Kessen, S.2    Kern, J.3    Zouni, A.4    Bittl, R.5
  • 143
    • 0000656545 scopus 로고
    • 2-state multiline signal from the photosynthetic oxygen-evolving complex
    • 2-State Multiline Signal from the Photosynthetic Oxygen-Evolving Complex. Biochemistry 28, 6954-6959 (1989)
    • (1989) Biochemistry , vol.28 , pp. 6954-6959
    • Haddy, A.1    Aasa, R.2    Andréasson, L.E.3
  • 145
    • 0032580791 scopus 로고    scopus 로고
    • 2-state multiline EPR signal in oriented photosystem II membranes: Structural implications for the manganese cluster in an oxygen- evolving complex
    • DOI 10.1021/bi973057f
    • 2-state multiline EPR signal in oriented photosystem II membranes: structural implications for the manganese cluster in an oxygen-evolving complex. Biochemistry 37, 9457-9465 (1998) (Pubitemid 28307702)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9457-9465
    • Hasegawa, K.1    Kusunoki, M.2    Inoue, Y.3    Ono, T.-A.4
  • 147
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem ii preparation from
    • D. A. Berthold, G. T. Babcock and C. F. Yocum: A Highly Resolved, Oxygen-Evolving Photosystem II Preparation from Spinach Thylakoid Membranes - EPR and Electron-Transport Properties. FEBS Lett 134, 231-234 (1981)
    • (1981) FEBS Lett , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 149
    • 46549097183 scopus 로고
    • Orientation of EPR signals arising from components in photosystem II membranes
    • A. W. Rutherford: Orientation of EPR Signals Arising from Components in Photosystem II Membranes. Biochim Biophys Acta 807, 189-201 (1985)
    • (1985) Biochim Biophys Acta , vol.807 , pp. 189-201
    • Rutherford, A.W.1
  • 150
    • 4243989332 scopus 로고
    • 2 state of the oxygen-evolving complex of photosystem II
    • 2 State of the Oxygen-Evolving Complex of Photosystem II. Biochemistry 25, 4609-4615 (1986)
    • (1986) Biochemistry , vol.25 , pp. 4609-4615
    • Zimmermann, J.L.1    Rutherford, A.W.2
  • 151
    • 0000916894 scopus 로고
    • 2 state of the photosynthetic oxygen-evolving complex arises from a multinuclear mn cluster
    • 2 State of the Photosynthetic Oxygen-Evolving Complex Arises from a Multinuclear Mn Cluster. J Am Chem Soc 112, 9389-9391 (1990)
    • (1990) J Am Chem Soc , vol.112 , pp. 9389-9391
    • Kim, D.H.1    Britt, R.D.2    Klein, M.P.3    Sauer, K.4
  • 152
    • 0026502425 scopus 로고
    • The manganese site of the photosynthetic oxygen-evolving complex probed by EPR spectroscopy of oriented photosystem II membranes: The g = 4 and g = 2 multiline signals
    • D. H. Kim, R. D. Britt, M. P. Klein and K. Sauer: The Manganese Site of the Photosynthetic Oxygen-Evolving Complex Probed by EPR Spectroscopy of Oriented Photosystem II Membranes: The g = 4 and g = 2 Multiline Signals. Biochemistry 31, 541-547 (1992)
    • (1992) Biochemistry , vol.31 , pp. 541-547
    • Kim, D.H.1    Britt, R.D.2    Klein, M.P.3    Sauer, K.4
  • 153
    • 0001069763 scopus 로고
    • Pulsed EPR study of Manganese g = 4.1 signal in plant photosystem II
    • A. V. Astashkin, Y. Kodera and A. Kawamori: Pulsed EPR Study of Manganese g = 4.1 Signal in Plant Photosystem II. J Magn Reson B 105, 113-119 (1994)
    • (1994) J Magn Reson B , vol.105 , pp. 113-119
    • Astashkin, A.V.1    Kodera, Y.2    Kawamori, A.3
  • 155
    • 16644369933 scopus 로고    scopus 로고
    • 2 state of photosystem II confirms an S = 5/2 origin of the X-band g = 4.1 signal
    • 2 state of photosystem II confirms an S = 5/2 origin of the X-band g = 4.1 signal. Biophys J 87, 2885-2896 (2004)
    • (2004) Biophys J , vol.87 , pp. 2885-2896
    • Haddy, A.1    Lakshmi, K.V.2    Brudvig, G.W.3    Frank, H.A.4
  • 156
    • 0036324367 scopus 로고    scopus 로고
    • 550 content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex
    • DOI 10.1023/A:1016140902662
    • K. V. Lakshmi, M. J. Reifler, D. A. Chisholm, J. Y. Wang, B. A. Diner and G. W. Brudvig: Correlation of the cytochrome c550 content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex. Photosynth Res 72, 175-189 (2002) (Pubitemid 34829498)
    • (2002) Photosynthesis Research , vol.72 , Issue.2 , pp. 175-189
    • Lakshmi, K.V.1    Reifler, M.J.2    Chisholm, D.A.3    Wang, J.Y.4    Diner, B.A.5    Brudvig, G.W.6
  • 157
    • 38049015832 scopus 로고    scopus 로고
    • 2 evolving complex
    • 2 evolving complex. Coord Chem Rev 252, 296-305 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 296-305
    • Yocum, C.F.1
  • 158
    • 0030736075 scopus 로고    scopus 로고
    • 0 state of the oxygen evolving complex in photosystem II
    • DOI 10.1021/bi971815w
    • 0 state of the oxygen evolving complex in photosystem II. Biochemistry 36, 13148-13152 (1997) (Pubitemid 27473358)
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13148-13152
    • Ahrling, K.A.1    Peterson, S.2    Styring, S.3
  • 160
    • 0033554388 scopus 로고    scopus 로고
    • Detection of an electron paramagnetic resonance signal in the S0 state of the manganese complex of photosystem II from Synechococcus elongatus
    • A. Boussac, H. Kuhl, E. Ghibaudi, M. Rögner and A. W. Rutherford: Detection of an electron paramagnetic resonance signal in the S0 state of the manganese complex of photosystem II from Synechococcus elongatus. Biochemistry 38, 11942-11948 (1999)
    • (1999) Biochemistry , vol.38 , pp. 11942-11948
    • Boussac, A.1    Kuhl, H.2    Ghibaudi, E.3    Rögner, M.4    Rutherford, A.W.5
  • 161
    • 0032474286 scopus 로고    scopus 로고
    • The So state EPR signal from the Mn cluster in photosystem II arises from an isolated S = 1/4 ground state
    • DOI 10.1021/bi980117o
    • 0 state EPR signal from the Mn cluster in photosystem II arises from an isolated S = 1/2 ground state. Biochemistry 37, 8115-8120 (1998) (Pubitemid 28307073)
    • (1998) Biochemistry , vol.37 , Issue.22 , pp. 8115-8120
    • Ahrling, K.A.1    Peterson, S.2    Styring, S.3
  • 162
    • 0001723479 scopus 로고
    • 1 state of the photosynthetic oxygen-evolving complex
    • 1 State of the Photosynthetic Oxygen-Evolving Complex. J Am Chem Soc 114, 2821-2826 (1992)
    • (1992) J Am Chem Soc , vol.114 , pp. 2821-2826
    • Dexheimer, S.L.1    Klein, M.P.2
  • 163
    • 0033874086 scopus 로고    scopus 로고
    • Pulsed and parallel-polarization EPR characterization of the photosystem II oxygen-evolving complex
    • DOI 10.1146/annurev.biophys.29.1.463
    • R. D. Britt, J. M. Peloquin and K. A. Campbell: Pulsed and parallel-polarization EPR characterization of the photosystem II oxygen-evolving complex. Annu Rev Biophys Biomol Struct 29, 463-495 (2000) (Pubitemid 30599601)
    • (2000) Annual Review of Biophysics and Biomolecular Structure , vol.29 , pp. 463-495
    • Britt, R.D.1    Peloquin, J.M.2    Campbell, K.A.3
  • 164
    • 0030993047 scopus 로고    scopus 로고
    • 1-state manganese cluster in the photosynthetic oxygen- evolving system
    • DOI 10.1021/bi962791g
    • T. Yamauchi, H. Mino, T. Matsukawa, A. Kawamori and T. Ono: Parallel polarization electron paramagnetic resonance studies of the S1-state manganese cluster in the photosynthetic oxygen-evolving system. Biochemistry 36, 7520-7526 (1997) (Pubitemid 27262377)
    • (1997) Biochemistry , vol.36 , Issue.24 , pp. 7520-7526
    • Yamauchi, T.1    Mino, H.2    Matsukawa, T.3    Kawamori, A.4    Ono, T.-A.5
  • 169
    • 0034625108 scopus 로고    scopus 로고
    • 3 state of the oxygen-evolving complex. A broadened radical signal induced by low- temperature near-infrared light illumination
    • DOI 10.1021/bi000131c
    • 3 state of the oxygen-evolving complex. A broadened radical signal induced by lowtemperature near-infrared light illumination. Biochemistry 39, 5246-5254 (2000) (Pubitemid 30257062)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5246-5254
    • Ioannidis, N.1    Petrouleas, V.2
  • 177
    • 68349101932 scopus 로고    scopus 로고
    • Electronic structure of the tyrosine D radical and the water-splitting complex from pulsed ENDOR spectroscopy on photosystem II single crystals
    • C. Teutloff, S. Pudollek, S. Kessen, M. Broser, A. Zouni and R. Bittl: Electronic structure of the tyrosine D radical and the water-splitting complex from pulsed ENDOR spectroscopy on photosystem II single crystals. Phys Chem Chem Phys 11, 6715-6726 (2009)
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 6715-6726
    • Teutloff, C.1    Pudollek, S.2    Kessen, S.3    Broser, M.4    Zouni, A.5    Bittl, R.6
  • 178
    • 0015212656 scopus 로고
    • Action of low concentrations of hydroxylamine on oxygen evolved by chlorella and Spinach chloroplasts
    • B. Bouges: Action of Low Concentrations of Hydroxylamine on Oxygen Evolved by Chlorella and Spinach Chloroplasts. Biochim Biophys Acta 234, 103-112 (1971)
    • (1971) Biochim Biophys Acta , vol.234 , pp. 103-112
    • Bouges, B.1
  • 179
    • 0023657038 scopus 로고
    • Reactions of hydroxylamine with the electron-donor side of photosystem II
    • W. F. Beck and G. W. Brudvig: Reactions of hydroxylamine with the electron-donor side of photosystem II. Biochemistry 26, 8285-8295 (1987)
    • (1987) Biochemistry , vol.26 , pp. 8285-8295
    • Beck, W.F.1    Brudvig, G.W.2
  • 180
    • 0025739052 scopus 로고
    • Evidence for a chemical-reaction of hydroxylamine with the photosynthetic water splitting enzyme S in the dark - Possible states of manganese and water in the S-cycle
    • H. Kretschmann, S. Pauly and H. T. Witt: Evidence for a Chemical-Reaction of Hydroxylamine with the Photosynthetic Water Splitting Enzyme S in the Dark - Possible States of Manganese and Water in the S-Cycle. Biochim Biophys Acta 1059, 208-214 (1991)
    • (1991) Biochim Biophys Acta , vol.1059 , pp. 208-214
    • Kretschmann, H.1    Pauly, S.2    Witt, H.T.3
  • 181
    • 0001723480 scopus 로고
    • Reduced derivatives of the manganese cluster in the photosynthetic oxygen-evolving complex
    • P. J. Riggs, R. Mei, C. F. Yocum and J. E. Penner-Hahn: Reduced Derivatives of the Manganese Cluster in the Photosynthetic Oxygen-Evolving Complex. J Am Chem Soc 114, 10650-10651 (1992)
    • (1992) J Am Chem Soc , vol.114 , pp. 10650-10651
    • Riggs, P.J.1    Mei, R.2    Yocum, C.F.3    Penner-Hahn, J.E.4
  • 182
    • 0027377509 scopus 로고
    • Chemical reduction of the water splitting enzyme system of photosynthesis and its light-induced reoxidation characterized by optical and mass spectrometric measurements: A basis for the estimation of the states of the redox active manganese and of water in the quaternary oxygen-evolving S-state cycle
    • DOI 10.1016/0005-2728(93)90118-Y
    • H. Kretschmann and H. T. Witt: Chemical-Reduction of the Water-Splitting Enzyme-System of Photosynthesis and Its Light-Induced Reoxidation Characterized by Optical and Mass-Spectrometric Measurements - a Basis for the Estimation of the States of the Redox Active Manganese and of Water in the Quaternary Oxygen-Evolving S-State Cycle. Biochim Biophys Acta 1144, 331-345 (1993) (Pubitemid 23290261)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1144 , Issue.3 , pp. 331-345
    • Kretschmann, H.1    Witt, H.T.2
  • 183
    • 0027384113 scopus 로고
    • -2 of the water oxidase in isolated spinach thylakoids
    • -2 of the water oxidase in isolated spinach thylakoids. Biochemistry 32, 9379-9386 (1993) (Pubitemid 23292057)
    • (1993) Biochemistry , vol.32 , Issue.36 , pp. 9379-9386
    • Messinger, J.1    Renger, G.2
  • 186
    • 0026739858 scopus 로고
    • 2+ formation and activity inhibition
    • 2+ Formation and Activity Inhibition. Biochemistry 31, 8449-8454 (1992)
    • (1992) Biochemistry , vol.31 , pp. 8449-8454
    • Mei, R.1    Yocum, C.F.2
  • 189
    • 0025099299 scopus 로고
    • Formation by NO of nitrosyl adducts of redox components of the photosystem II reaction center. I. NO binds to the acceptor-side non-heme iron
    • V. Petrouleas and B. A. Diner: Formation by NO of Nitrosyl Adducts of Redox Components of the Photosystem II Reaction Center. I. NO Binds to the Acceptor-Side Non-Heme Iron. Biochim Biophys Acta 1015, 131-140 (1990)
    • (1990) Biochim Biophys Acta , vol.1015 , pp. 131-140
    • Petrouleas, V.1    Diner, B.A.2
  • 191
    • 0031029894 scopus 로고    scopus 로고
    • No interacts with the tyrosine radical Y(D)· of photosystem II to form an iminoxyl radical
    • DOI 10.1021/bi9622074
    • D· of photosystem II to form an iminoxyl radical. Biochemistry 36, 1411-1417 (1997) (Pubitemid 27074965)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1411-1417
    • Sanakis, Y.1    Goussias, C.2    Mason, R.P.3    Petrouleas, V.4
  • 193
    • 0032540003 scopus 로고    scopus 로고
    • 1 the state of the water-oxidizing complex of photosystem II
    • DOI 10.1021/bi972828c
    • J. Sarrou, N. Ioannidis, Y. Deligiannakis and V. Petrouleas: A Mn(II)-Mn(III) EPR signal arises from the interaction of NO with the S1 state of the water-oxidizing complex of photosystem II. Biochemistry 37, 3581-3587 (1998) (Pubitemid 28162912)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3581-3587
    • Sarrou, J.1    Ioannidis, N.2    Deligiannakis, Y.3    Petrouleas, V.4
  • 194
    • 0032564444 scopus 로고    scopus 로고
    • -1 to the state characterized by the Mn(II)-Mn(III) multiline EPR signal
    • DOI 10.1021/bi981724e
    • 1 to the state characterized by the Mn(II)-Mn(III) multiline EPR signal. Biochemistry 37, 16445-16451 (1998) (Pubitemid 28543901)
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16445-16451
    • Ioannidis, N.1    Sarrou, J.2    Schansker, G.3    Petrouleas, V.4
  • 196
    • 0034044161 scopus 로고    scopus 로고
    • Interaction of nitric oxide with the oxygen evolving complex of photosystem II and manganese catalase: A comparative study
    • N. Ioannidis, G. Schansker, V. V. Barynin and V. Petrouleas: Interaction of nitric oxide with the oxygen evolving complex of photosystem II and manganese catalase: a comparative study. J Biol Inorg Chem 5, 354-363 (2000) (Pubitemid 30407894)
    • (2000) Journal of Biological Inorganic Chemistry , vol.5 , Issue.3 , pp. 354-363
    • Ioannidis, N.1    Schansker, G.2    Barynin, V.V.3    Petrouleas, V.4
  • 197
    • 0008796636 scopus 로고
    • 2-evolving complexes isolated from synechococcus
    • Ö. Saygin and H. T. Witt: On the Change of the Charges in the four Photo-induced Oxidation Steps of the Water-Splitting Enzyme System S - Optical Characterization at O2-Evolving Complexes Isolated from Synechococcus. FEBS Lett 176, 83-87 (1984)
    • (1984) FEBS Lett , vol.176 , pp. 83-87
    • Saygin, O.1    Witt, H.T.2
  • 198
    • 46549094068 scopus 로고
    • Evidence for the electrochromic identification of the change of charges in the four oxidation steps of the photoinduced water cleavage in photosynthesis
    • Ö. Saygin and H. T. Witt: Evidence for the Electrochromic Identification of the Change of Charges in the four Oxidation Steps of the Photoinduced Water Cleavage in Photosynthesis. FEBS Lett 187, 224-226 (1985)
    • (1985) FEBS Lett , vol.187 , pp. 224-226
    • Saygin, O.1    Witt, H.T.2
  • 200
    • 69849088750 scopus 로고    scopus 로고
    • Probing the accessibility of the Mn4Ca cluster in photosystem II: Channels calculation, noble gas derivatization, and cocrystallization with DMSO
    • A. Gabdulkhakov, A. Guskov, M. Broser, J. Kern, F. Müh, W. Saenger and A. Zouni: Probing the Accessibility of the Mn4Ca Cluster in Photosystem II: Channels Calculation, Noble Gas Derivatization, and Cocrystallization with DMSO. Structure 17, 1223-1234 (2009)
    • (2009) Structure , vol.17 , pp. 1223-1234
    • Gabdulkhakov, A.1    Guskov, A.2    Broser, M.3    Kern, J.4    Müh, F.5    Saenger, W.6    Zouni, A.7
  • 201
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • A. A. Vaguine, J. Richelle and S. J. Wodak: SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D 55, 191-205 (1999) (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 202
    • 33749179561 scopus 로고    scopus 로고
    • Radiation damage in macromolecular cryocrystallography
    • DOI 10.1016/j.sbi.2006.08.001, PII S0959440X06001369, Carbohydrates and Glycoconjugates / Biophysical Methods
    • R. B. G. Ravelli and E. F. Garman: Radiation damage in macromolecular cryocrystallography. Curr Opin Struct Biol 16, 624-629 (2006) (Pubitemid 44472608)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 624-629
    • Ravelli, R.B.1    Garman, E.F.2
  • 204
    • 4444294012 scopus 로고    scopus 로고
    • Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
    • DOI 10.1016/j.str.2004.07.013, PII S0969212604002825
    • V. Adam, A. Royant, V. Nivière, F. P. Molina-Heredia and D. Bourgeois: Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction. Structure 12, 1729-1740 (2004) (Pubitemid 39200524)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1729-1740
    • Adam, V.1    Royant, A.2    Niviere, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 205
    • 11244354296 scopus 로고    scopus 로고
    • Specific radiation damage illustrates light-induced structural changes in the photosynthetic reaction center
    • DOI 10.1021/ja0448115
    • R. H. Baxter, B. L. Seagle, N. Ponomarenko and J. R. Norris: Specific radiation damage illustrates lightinduced structural changes in the photosynthetic reaction center. J Am Chem Soc 126, 16728-16729 (2004) (Pubitemid 40069484)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.51 , pp. 16728-16729
    • Baxter, R.H.G.1    Seagle, B.-L.2    Ponomarenko, N.3    Norris, J.R.4
  • 207
    • 50849108837 scopus 로고    scopus 로고
    • Electron paramagnetic resonance study of radiation damage in photosynthetic reaction center crystals
    • L. M. Utschig, S. D. Chemerisov, D. M. Tiede and O. G. Poluektov: Electron paramagnetic resonance study of radiation damage in photosynthetic reaction center crystals. Biochemistry 47, 9251-9257 (2008)
    • (2008) Biochemistry , vol.47 , pp. 9251-9257
    • Utschig, L.M.1    Chemerisov, S.D.2    Tiede, D.M.3    Poluektov, O.G.4
  • 208
    • 8144226211 scopus 로고    scopus 로고
    • 1-state - EXAFS results in relation to recent crystallographic data
    • 1-state - EXAFS results in relation to recent crystallographic data. Phys Chem Chem Phys 6, 4781-4792 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4781-4792
    • Dau, H.1    Liebisch, P.2    Haumann, M.3
  • 210
    • 33645219974 scopus 로고    scopus 로고
    • Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K
    • DOI 10.1074/jbc.M509724200
    • M. Grabolle, M. Haumann, C. Müller, P. Liebisch and H. Dau: Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by Xray irradiation at 10-300 K. J Biol Chem 281, 4580-4588 (2006) (Pubitemid 43847716)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 4580-4588
    • Grabolle, M.1    Haumann, M.2    Muller, C.3    Liebisch, P.4    Dau, H.5
  • 211
    • 73549096645 scopus 로고    scopus 로고
    • Quantum chemistry as a tool in bioenergetics
    • M. R. Blomberg and P. E. Siegbahn: Quantum chemistry as a tool in bioenergetics. Biochim Biophys Acta 1797, 129-142 (2010)
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 129-142
    • Blomberg, M.R.1    Siegbahn, P.E.2
  • 212
    • 34249858864 scopus 로고    scopus 로고
    • 4Ca cluster
    • DOI 10.1016/j.bbabio.2007.03.012, PII S0005272807000795, Structure and Function of Photosystems
    • 4Ca cluster. Biochim Biophys Acta 1767, 484-492 (2007) (Pubitemid 46860311)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 484-492
    • Kusunoki, M.1
  • 213
    • 36149024213 scopus 로고
    • Anomalous dispersion and scattering of X-rays
    • L. G. Parratt and C. F. Hempstead: Anomalous Dispersion and Scattering of X-Rays. Phys Rev 94, 1593-1600 (1954)
    • (1954) Phys Rev , vol.94 , pp. 1593-1600
    • Parratt, L.G.1    Hempstead, C.F.2
  • 214
    • 0001327635 scopus 로고
    • Synchrotron X-radiation protein crystallography - Instrumentation, methods and applications
    • J. R. Helliwell: Synchrotron X-Radiation Protein Crystallography - Instrumentation, Methods and Applications. Rep Prog Phys 47, 1403-1497 (1984)
    • (1984) Rep Prog Phys , vol.47 , pp. 1403-1497
    • Helliwell, J.R.1
  • 217
    • 0040070502 scopus 로고    scopus 로고
    • Manganese cluster in photosynthesis: Where plants oxidize water to dioxygen
    • V. K. Yachandra, K. Sauer and M. P. Klein: Manganese cluster in photosynthesis: Where plants oxidize water to dioxygen. Chem Rev 96, 2927-2950 (1996) (Pubitemid 126641122)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2927-2950
    • Yachandra, V.K.1    Sauer, K.2    Klein, M.P.3
  • 218
    • 33845556217 scopus 로고
    • State of manganese in the photosynthetic apparatus. 1. Extended X-ray absorption fine-structure studies on chloroplasts and Di-μ-oxo-bridged dimanganese model compounds
    • J. A. Kirby, A. S. Robertson, J. P. Smith, A. C. Thompson, S. R. Cooper and M. P. Klein: State of Manganese in the Photosynthetic Apparatus. 1. Extended X-Ray Absorption Fine-Structure Studies on Chloroplasts and Di-μ-Oxo-Bridged Dimanganese Model Compounds. J Am Chem Soc 103, 5529-5537 (1981)
    • (1981) J Am Chem Soc , vol.103 , pp. 5529-5537
    • Kirby, J.A.1    Robertson, A.S.2    Smith, J.P.3    Thompson, A.C.4    Cooper, S.R.5    Klein, M.P.6
  • 219
    • 84990166672 scopus 로고
    • The active-sites in manganese-containing metalloproteins and inorganic model complexes
    • K. Wieghardt: The Active-Sites in Manganese-Containing Metalloproteins and Inorganic Model Complexes. Angew Chem Int Ed 28, 1153-1172 (1989)
    • (1989) Angew Chem Int Ed , vol.28 , pp. 1153-1172
    • Wieghardt, K.1
  • 220
    • 33845182806 scopus 로고
    • Manganese carboxylate chemistry and its biological relevance
    • G. Christou: Manganese Carboxylate Chemistry and Its Biological Relevance. Acc Chem Res 22, 328-335 (1989)
    • (1989) Acc Chem Res , vol.22 , pp. 328-335
    • Christou, G.1
  • 221
    • 12044259187 scopus 로고
    • Interaction of manganese with dioxygen and its reduced derivatives
    • V. L. Pecoraro, M. J. Baldwin and A. Gelasco: Interaction of Manganese with Dioxygen and Its Reduced Derivatives. Chem Rev 94, 807-826 (1994) (Pubitemid 24987712)
    • (1994) Chemical Reviews , vol.94 , Issue.3 , pp. 807-826
    • Pecoraro, V.L.1    Baldwin, M.J.2    Gelasco, A.3
  • 222
  • 226
    • 1942440428 scopus 로고    scopus 로고
    • The water-oxidation complex in photosynthesis
    • DOI 10.1016/j.bbabio.2003.07.004, PII S0005272803002081
    • K. Sauer and V. K. Yachandra: The water-oxidation complex in photosynthesis. Biochim Biophys Acta 1655, 140-148 (2004) (Pubitemid 38526174)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 140-148
    • Sauer, K.1    Yachandra, V.K.2
  • 227
    • 0024966057 scopus 로고
    • The manganese site of the photosynthetic water-splitting enzyme
    • G. N. George, R. C. Prince and S. P. Cramer: The Manganese Site of the Photosynthetic Water-Splitting Enzyme. Science 243, 789-791 (1989)
    • (1989) Science , vol.243 , pp. 789-791
    • George, G.N.1    Prince, R.C.2    Cramer, S.P.3
  • 228
    • 0027989783 scopus 로고
    • Orientation of the oxygen-evolving manganese complex in a photosystem II membrane preparation: An X-ray absorption spectroscopy study
    • I. Mukerji, J. C. Andrews, V. J. Derose, M. J. Latimer, V. K. Yachandra, K. Sauer and M. P. Klein: Orientation of the Oxygen-Evolving Manganese Complex in a Photosystem II: Membrane Preparation - an X-Ray Absorption Spectroscopy Study. Biochemistry 33, 9712-9721 (1994) (Pubitemid 24272932)
    • (1994) Biochemistry , vol.33 , Issue.32 , pp. 9712-9721
    • Mukerji, I.1    Andrews, J.C.2    DeRose, V.J.3    Latimer, M.J.4    Yachandra, V.K.5    Sauer, K.6    Klein, M.P.7
  • 229
    • 0032546622 scopus 로고    scopus 로고
    • Structure and orientation of the oxygen-evolving manganese complex of green algae and higher plants investigated by X-ray absorption linear dichroism spectroscopy on oriented photosystem II membrane particles
    • DOI 10.1021/bi972329b
    • H. Schiller, J. Dittmer, L. Iuzzolino, W. Dorner, W. Meyer-Klaucke, V. A. Sole, H. F. Nolting and H. Dau: Structure and orientation of the oxygen-evolving manganese complex of green algae and higher plants investigated by Xray absorption linear dichroism spectroscopy on oriented photosystem II membrane particles. Biochemistry 37, 7340-7350 (1998) (Pubitemid 28235217)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7340-7350
    • Schiller, H.1    Dittmer, J.2    Iuzzolino, L.3    Dorner, W.4    Meyer-Klaucke, W.5    Sole, V.A.6    Nolting, H.-F.7    Dau, H.8
  • 231
    • 77951189303 scopus 로고    scopus 로고
    • Linear dichroism in the XANES of partially oriented samples: Theory and application to the photosynthetic manganese complex
    • P. Liebisch and H. Dau: Linear Dichroism in the XANES of Partially Oriented Samples: Theory and Application to the Photosynthetic Manganese Complex. ChemPhysChem 11, 1236-1247 (2010)
    • (2010) ChemPhysChem , vol.11 , pp. 1236-1247
    • Liebisch, P.1    Dau, H.2
  • 232
    • 41449116568 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II
    • DOI 10.1021/ja076130q
    • E. M. Sproviero, J. A. Gascón, J. P. McEvoy, G. W. Brudvig and V. S. Batista: Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II. J Am Chem Soc 130, 3428-3442 (2008) (Pubitemid 351456044)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.11 , pp. 3428-3442
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 233
    • 44349142690 scopus 로고    scopus 로고
    • A model of the oxygen-evolving center of photosystem II predicted by structural refinement based on EXAFS simulations
    • DOI 10.1021/ja801979n
    • E. M. Sproviero, J. A. Gascón, J. P. McEvoy, G. W. Brudvig and V. S. Batista: A model of the oxygen-evolving center of photosystem II predicted by structural refinement based on EXAFS simulations. J Am Chem Soc 130, 6728-6730 (2008) (Pubitemid 351748407)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.21 , pp. 6728-6730
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 234
    • 76149092480 scopus 로고    scopus 로고
    • The MoD-QM/MM methodology for structural refinement of photosystem II and other biological macromolecules
    • E. M. Sproviero, M. B. Newcomer, J. A. Gascón, E. R. Batista, G. W. Brudvig and V. S. Batista: The MoD-QM/MM methodology for structural refinement of photosystem II and other biological macromolecules. Photosynth Res 102, 455-470 (2009)
    • (2009) Photosynth Res , vol.102 , pp. 455-470
    • Sproviero, E.M.1    Newcomer, M.B.2    Gascón, J.A.3    Batista, E.R.4    Brudvig, G.W.5    Batista, V.S.6
  • 236
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM methods for biomolecular systems
    • H. M. Senn and W. Thiel: QM/MM Methods for Biomolecular Systems. Angew Chem Int Ed 48, 1198-1229 (2009)
    • (2009) Angew Chem Int Ed , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 238
    • 0035808693 scopus 로고    scopus 로고
    • The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation
    • G. M. Ananyev, L. Zaltsman, C. Vasko and G. C. Dismukes: The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation. Biochim Biophys Acta 1503, 52-68 (2001)
    • (2001) Biochim Biophys Acta , vol.1503 , pp. 52-68
    • Ananyev, G.M.1    Zaltsman, L.2    Vasko, C.3    Dismukes, G.C.4
  • 239
    • 8144226360 scopus 로고    scopus 로고
    • D1 protein processing and Mn cluster assembly in light of the emerging Photosystem II structure
    • R. L. Burnap: D1 protein processing and Mn cluster assembly in light of the emerging Photosystem II structure. Phys Chem Chem Phys 6, 4803-4809 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4803-4809
    • Burnap, R.L.1
  • 241
    • 38049100652 scopus 로고    scopus 로고
    • Photoassembly of the water-oxidizing complex in photosystem II
    • J. Dasgupta, G. M. Ananyev and G. C. Dismukes: Photoassembly of the Water-Oxidizing Complex in Photosystem II. Coord Chem Rev 252, 347-360 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 347-360
    • Dasgupta, J.1    Ananyev, G.M.2    Dismukes, G.C.3
  • 242
    • 0025925201 scopus 로고
    • 2+ binding to photosystem II
    • 2+ Binding to Photosystem II. Biochemistry 30, 7836-7842 (1991)
    • (1991) Biochemistry , vol.30 , pp. 7836-7842
    • Mei, R.1    Yocum, C.F.2
  • 243
    • 0007728404 scopus 로고
    • 2-Evolving complex of photosystem II
    • 2-Evolving Complex of Photosystem II. Photosynth Res 38, 449-453 (1993)
    • (1993) Photosynth Res , vol.38 , pp. 449-453
    • Mei, R.1    Yocum, C.2
  • 244
    • 8144221719 scopus 로고    scopus 로고
    • Probing reactive sites within the Photosystem II manganese cluster: Evidence for separate populations of manganese that differ in redox potential
    • T. Kuntzleman, M. McCarrick, J. Penner-Hahn and C. Yocum: Probing reactive sites within the Photosystem II manganese cluster: Evidence for separate populations of manganese that differ in redox potential. Phys Chem Chem Phys 6, 4897-4904 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4897-4904
    • Kuntzleman, T.1    McCarrick, M.2    Penner-Hahn, J.3    Yocum, C.4
  • 245
    • 0037195245 scopus 로고    scopus 로고
    • Calcium EXAFS establishes the Mn-Ca cluster in the oxygen-evolving complex of photosystem II
    • DOI 10.1021/bi026569p
    • R. M. Cinco, K. L. M. Holman, J. H. Robblee, J. Yano, S. A. Pizarro, E. Bellacchio, K. Sauer and V. K. Yachandra: Calcium EXAFS establishes the Mn-Ca cluster in the oxygen-evolving complex of photosystem II. Biochemistry 41, 12928-12933 (2002) (Pubitemid 35215775)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12928-12933
    • Cinco, R.M.1    Holman, K.L.M.2    Robblee, J.H.3    Yano, J.4    Pizarro, S.A.5    Bellacchio, E.6    Sauer, K.7    Yachandra, V.K.8
  • 246
    • 0000981541 scopus 로고
    • Calcium reconstitutes high-rates of oxygen evolution in polypeptide depleted photosystem II preparations
    • D. F. Ghanotakis, G. T. Babcock and C. F. Yocum: Calcium Reconstitutes High-Rates of Oxygen Evolution in Polypeptide Depleted Photosystem II Preparations. FEBS Lett 167, 127-130 (1984)
    • (1984) FEBS Lett , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 247
    • 0034719030 scopus 로고    scopus 로고
    • z· in PSII membranes - Evidence for concerted hydrogen-atom transfer in oxygen evolution
    • DOI 10.1021/bi0018077
    • Z· in PSII membranes - Evidence for concerted hydrogen-atom transfer in oxygen evolution. Biochemistry 39, 16220-16229 (2000) (Pubitemid 32038286)
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 16220-16229
    • Westphal, K.L.1    Lydakis-Simantiris, N.2    Cukier, R.I.3    Babcock, G.T.4
  • 252
    • 34249807336 scopus 로고    scopus 로고
    • Purification, crystallization and X-ray diffraction analyses of the T. elongatus PSII core dimer with strontium replacing calcium in the oxygen-evolving complex
    • DOI 10.1016/j.bbabio.2007.01.007, PII S0005272807000102, Structure and Function of Photosystems
    • J. Kargul, K. Maghlaoul, J. W. Murray, Z. Deak, A. Boussac, A. W. Rutherford, I. Vass and J. Barber: Purification, crystallization and X-ray diffraction analyses of the T. elongatus PSII core dimer with strontium replacing calcium in the oxygen-evolving complex. Biochim Biophys Acta 1767, 404-413 (2007) (Pubitemid 46855740)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 404-413
    • Kargul, J.1    Maghlaoui, K.2    Murray, J.W.3    Deak, Z.4    Boussac, A.5    William Rutherford, A.6    Vass, I.7    Barber, J.8
  • 254
    • 53849139144 scopus 로고    scopus 로고
    • A structure-consistent mechanism for dioxygen formation in photosystem II
    • E. M. Siegbahn: A Structure-Consistent Mechanism for Dioxygen Formation in Photosystem II. Chem Eur J 14, 8290-8302 (2008)
    • (2008) Chem Eur J , vol.14 , pp. 8290-8302
    • Siegbahn, E.M.1
  • 255
    • 42149103898 scopus 로고    scopus 로고
    • Theoretical studies of O-O bond formation in photosystem II
    • P. E. M. Siegbahn: Theoretical studies of O-O bond formation in photosystem II. Inorg Chem 47, 1779-1786 (2008)
    • (2008) Inorg Chem , vol.47 , pp. 1779-1786
    • Siegbahn, P.E.M.1
  • 256
    • 72749109576 scopus 로고    scopus 로고
    • Water oxidation in photosystem II: Oxygen release, proton release and the effect of chloride
    • P. E. Siegbahn: Water oxidation in photosystem II: oxygen release, proton release and the effect of chloride. Dalton Trans 10063-10068 (2009)
    • (2009) Dalton Trans , pp. 10063-10068
    • Siegbahn, P.E.1
  • 257
    • 0026569892 scopus 로고
    • Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster
    • P. J. Nixon and B. A. Diner: Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster. Biochemistry 31, 942-948 (1992)
    • (1992) Biochemistry , vol.31 , pp. 942-948
    • Nixon, P.J.1    Diner, B.A.2
  • 258
    • 0028303152 scopus 로고
    • Site-directed photosystem II mutants with perturbed oxygen-evolving properties. 1. Instability or inefficient assembly of the manganese cluster in vivo
    • DOI 10.1021/bi00186a013
    • H. A. Chu, A. P. Nguyen and R. J. Debus: Site-Directed Photosystem II Mutants with Perturbed Oxygen-Evolving Properties. 1. Instability or Inefficient Assembly of the Manganese Cluster in vivo. Biochemistry 33, 6137-6149 (1994) (Pubitemid 24190765)
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6137-6149
    • Chu, H.-A.1    Nguyen, A.P.2    Debus, R.J.3
  • 259
    • 0029033834 scopus 로고
    • Amino-acid-residues that influence the binding of manganese or calcium to photosystem II. 1. The lumenal interhelical domains of the D1 polypeptide
    • H. A. Chu, A. P. Nguyen and R. J. Debus: Amino-Acid-Residues That Influence the Binding of Manganese or Calcium to Photosystem II. 1. The Lumenal Interhelical Domains of the D1 Polypeptide. Biochemistry 34, 5839-5858 (1995)
    • (1995) Biochemistry , vol.34 , pp. 5839-5858
    • Chu, H.A.1    Nguyen, A.P.2    Debus, R.J.3
  • 260
    • 0026635213 scopus 로고
    • 2+ is slowed in a site-directed mutant, at aspartate 170 of polypeptide D1 of photosystem II, inactive for photosynthetic oxygen evolution
    • 2+ Is Slowed in a Site-Directed Mutant, at Aspartate 170 of Polypeptide D1 of Photosystem II, Inactive for Photosynthetic Oxygen Evolution. Biochim Biophys Acta 1101, 134-138 (1992)
    • (1992) Biochim Biophys Acta , vol.1101 , pp. 134-138
    • Diner, B.A.1    Nixon, P.J.2
  • 261
    • 0028985255 scopus 로고
    • Assembly of the photosystem II oxygenevolving complex is inhibited in psbA site-directed mutants of Chlamydomonas reinhardtii. Aspartate 170 of the D1 polypeptide
    • J. P. Whitelegge, D. Koo, B. A. Diner, I. Domian and J. M. Erickson: Assembly of the Photosystem II oxygenevolving complex is inhibited in psbA site-directed mutants of Chlamydomonas reinhardtii. Aspartate 170 of the D1 polypeptide. J Biol Chem 270, 225-35 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 225-235
    • Whitelegge, J.P.1    Koo, D.2    Diner, B.A.3    Domian, I.4    Erickson, J.M.5
  • 262
    • 38049029119 scopus 로고    scopus 로고
    • Protein ligation of the photosynthetic oxygen-evolving center
    • R. J. Debus: Protein ligation of the photosynthetic oxygen-evolving center. Coord Chem Rev 252, 244-258 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 244-258
    • Debus, R.J.1
  • 263
    • 0041317461 scopus 로고    scopus 로고
    • Does aspartate 170 of the D1 polypeptide ligate the manganese cluster in photosystem II? An EPR and ESEEM study
    • DOI 10.1021/bi034859f
    • R. J. Debus, C. Aznar, K. A. Campbell, W. Gregor, B. A. Diner and R. D. Britt: Does aspartate 170 of the D1 polypeptide ligate the manganese cluster in photosystem II? An EPR and ESEEM Study. Biochemistry 42, 10600-10608 (2003) (Pubitemid 37102098)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10600-10608
    • Debus, R.J.1    Aznar, C.2    Campbell, K.A.3    Gregor, W.4    Diner, B.A.5    Britt, R.D.6
  • 264
    • 33947539623 scopus 로고    scopus 로고
    • Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution
    • DOI 10.1007/s11120-007-9137-5
    • T. Noguchi: Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution. Photosynth Res 91, 59-69 (2007) (Pubitemid 46466318)
    • (2007) Photosynthesis Research , vol.91 , Issue.1 , pp. 59-69
    • Noguchi, T.1
  • 265
    • 38049004891 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of the photosynthetic oxygen-evolving center
    • T. Noguchi: Fourier transform infrared analysis of the photosynthetic oxygen-evolving center. Coord Chem Rev 252, 336-346 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 336-346
    • Noguchi, T.1
  • 266
    • 0035916217 scopus 로고    scopus 로고
    • D1-Asp170 Is structurally coupled to the oxygen evolving complex in photosystem II as revealed by light-induced fourier transform infrared difference spectroscopy
    • DOI 10.1021/bi0022994
    • H. A. Chu, R. J. Debus and G. T. Babcock: D1-Asp170 is structurally coupled to the oxygen evolving complex in photosystem II as revealed by light-induced Fourier transform infrared difference spectroscopy. Biochemistry 40, 2312-2316 (2001) (Pubitemid 32165703)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2312-2316
    • Chu, H.-A.1    Debus, R.J.2    Babcock, G.T.3
  • 268
    • 0034732948 scopus 로고    scopus 로고
    • Glutamate 189 of the D1 polypeptide modulates the magnetic and redox properties of the manganese cluster and tyrosine Y(Z) in photosystem II
    • DOI 10.1021/bi992749w
    • Z in photosystem II. Biochemistry 39, 6275-6287 (2000) (Pubitemid 30347131)
    • (2000) Biochemistry , vol.39 , Issue.21 , pp. 6275-6287
    • Debus, R.J.1    Campbell, K.A.2    Pham, D.P.3    Hays, A.-M.A.4    Britt, R.D.5
  • 269
    • 0035519286 scopus 로고    scopus 로고
    • Photosynthetic water oxidation in Synechocystis sp. PCC6803: Mutations D1-E189K, R and Q are without influence on electron transfer at the donor side of photosystem II
    • DOI 10.1016/S0005-2728(01)00217-1, PII S0005272801002171
    • J. Clausen, S. Winkler, A. M. Hays, M. Hundelt, R. J. Debus and W. Junge: Photosynthetic water oxidation in Synechocystis sp. PCC6803: mutations D1-E189K, R and Q are without influence on electron transfer at the donor side of photosystem II. Biochim Biophys Acta 1506, 224-235 (2001) (Pubitemid 34075233)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1506 , Issue.3 , pp. 224-235
    • Clausen, J.1    Winkler, S.2    Hays, A.-M.A.3    Hundelt, M.4    Debus, R.J.5    Junge, W.6
  • 270
    • 27844436623 scopus 로고    scopus 로고
    • Changes in structural and functional properties of oxygen-evolving complex induced by replacement of D1-glutamate 189 with glutamine in photosystem II: Ligation of glutamate 189 carboxylate to the manganese cluster
    • DOI 10.1074/jbc.M505887200
    • Y. Kimura, N. Mizusawa, A. Ishii, S. Nakazawa and T. A. Ono: Changes in structural and functional properties of oxygen-evolving complex induced by replacement of D1-glutamate 189 with glutamine in photosystem II: ligation of glutamate 189 carboxylate to the manganese cluster. J Biol Chem 280, 37895-37900 (2005) (Pubitemid 41642401)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37895-37900
    • Kimura, Y.1    Mizusawa, N.2    Ishii, A.3    Nakazawa, S.4    Ono, T.-A.5
  • 271
    • 33746303803 scopus 로고    scopus 로고
    • 3 transitions in photosystem II
    • DOI 10.1021/bi060583a
    • 3 transitions in photosystem II. Biochemistry 45, 8801-8811 (2006) (Pubitemid 44102677)
    • (2006) Biochemistry , vol.45 , Issue.29 , pp. 8801-8811
    • Strickler, M.A.1    Hillier, W.2    Debus, R.J.3
  • 273
    • 0029071492 scopus 로고
    • Amino-acid-residues that influence the binding of manganese or calcium to photosystem II. 2. The carboxy-terminal domain of the D1 polypeptide
    • H. A. Chu, A. P. Nguyen and R. J. Debus: Amino-Acid-Residues That Influence the Binding of Manganese or Calcium to Photosystem II. 2. The Carboxy-Terminal Domain of the D1 Polypeptide. Biochemistry 34, 5859-5882 (1995)
    • (1995) Biochemistry , vol.34 , pp. 5859-5882
    • Chu, H.A.1    Nguyen, A.P.2    Debus, R.J.3
  • 274
    • 0035957275 scopus 로고    scopus 로고
    • Does histidine 332 of the D1 polypeptide ligate the manganese cluster in photosystem II? An electron spin echo envelope modulation study
    • DOI 10.1021/bi002394c
    • R. J. Debus, K. A. Campbell, W. Gregor, Z. L. Li, R. L. Burnap and R. D. Britt: Does histidine 332 of the D1 polypeptide ligate the manganese cluster in photosystem II? An electron spin echo envelope modulation study. Biochemistry 40, 3690-3699 (2001) (Pubitemid 32242827)
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3690-3699
    • Debus, R.J.1    Campbell, K.A.2    Gregor, W.3    Li, Z.-L.4    Burnap, R.L.5    Britt, R.D.6
  • 275
    • 0033520084 scopus 로고    scopus 로고
    • Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced Fourier transform infrared difference spectroscopy
    • T. Noguchi, Y. Inoue and X. S. Tang: Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced Fourier transform infrared difference spectroscopy. Biochemistry 38, 10187-10195 (1999)
    • (1999) Biochemistry , vol.38 , pp. 10187-10195
    • Noguchi, T.1    Inoue, Y.2    Tang, X.S.3
  • 276
    • 28944448293 scopus 로고    scopus 로고
    • FTIR detection of structural changes in a histidine ligand during S-state cycling of photosynthetic oxygen-evolving complex
    • DOI 10.1021/bi051306r
    • Y. Kimura, N. Mizusawa, A. Ishii and T. Ono: FTIR detection of structural changes in a histidine ligand during S-state cycling of photosynthetic oxygen-evolving complex. Biochemistry 44, 16072-16078 (2005) (Pubitemid 41785805)
    • (2005) Biochemistry , vol.44 , Issue.49 , pp. 16072-16078
    • Kimura, Y.1    Mizusawa, N.2    Ishii, A.3    Ono, T.-A.4
  • 278
    • 41249098659 scopus 로고    scopus 로고
    • Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongatus
    • M. Sugiura, A. Boussac, T. Noguchi and F. Rappaport: Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongatus. Biochim Biophys Acta 1777, 331-342 (2008)
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 331-342
    • Sugiura, M.1    Boussac, A.2    Noguchi, T.3    Rappaport, F.4
  • 282
    • 0026453128 scopus 로고
    • Role of the carboxy terminus of polypeptide D1 in the assembly of a functional water-oxidizing manganese cluster in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Assembly requires a free carboxyl group at Cterminal position 344
    • P. J. Nixon, J. T. Trost and B. A. Diner: Role of the carboxy terminus of polypeptide D1 in the assembly of a functional water-oxidizing manganese cluster in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: assembly requires a free carboxyl group at Cterminal position 344. Biochemistry 31, 10859-10871 (1992)
    • (1992) Biochemistry , vol.31 , pp. 10859-10871
    • Nixon, P.J.1    Trost, J.T.2    Diner, B.A.3
  • 284
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • P. J. Nixon, F. Michoux, J. F. Yu, M. Boehm and J. Komenda: Recent advances in understanding the assembly and repair of photosystem II. Ann Bot 106, 1-16 (2010)
    • (2010) Ann Bot , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.F.3    Boehm, M.4    Komenda, J.5
  • 285
    • 1542638640 scopus 로고    scopus 로고
    • 2 Transition: An Isotope-Edited FTIR Study
    • DOI 10.1021/bi035915f
    • 2 transition: An isotope-edited FTIR study. Biochemistry 43, 3152-3166 (2004) (Pubitemid 38352265)
    • (2004) Biochemistry , vol.43 , Issue.11 , pp. 3152-3166
    • Chu, H.-A.1    Hillier, W.2    Debus, R.J.3
  • 286
    • 12544257799 scopus 로고    scopus 로고
    • Structural changes of D1 C-terminal alphacarboxylate during S-state cycling in photosynthetic oxygen evolution
    • Y. Kimura, N. Mizusawa, T. Yamanari, A. Ishii and T. Ono: Structural changes of D1 C-terminal alphacarboxylate during S-state cycling in photosynthetic oxygen evolution. J Biol Chem 280, 2078-2083 (2005)
    • (2005) J Biol Chem , vol.280 , pp. 2078-2083
    • Kimura, Y.1    Mizusawa, N.2    Yamanari, T.3    Ishii, A.4    Ono, T.5
  • 287
    • 20544470177 scopus 로고    scopus 로고
    • Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the C-terminus of the D1 polypeptide of photosystem II does not ligate calcium
    • DOI 10.1021/bi050653y
    • M. A. Strickler, L. M. Walker, W. Hillier and R. J. Debus: Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the Cterminus of the D1 polypeptide of photosystem II does not ligate calcium. Biochemistry 44, 8571-8577 (2005) (Pubitemid 40840422)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8571-8577
    • Strickler, M.A.1    Walker, L.M.2    Hillier, W.3    Debus, R.J.4
  • 289
    • 0033619712 scopus 로고    scopus 로고
    • Site-directed mutagenesis of glutamate residues in the large extrinsic loop of the photosystem II protein CP 43 affects oxygen-evolving activity and PS II assembly
    • C. Rosenberg, J. Christian, T. M. Bricker and C. Putnam-Evans: Site-directed mutagenesis of glutamate residues in the large extrinsic loop of the photosystem II protein CP 43 affects oxygen-evolving activity and PS II assembly. Biochemistry 38, 15994-6000 (1999) (Pubitemid 129520494)
    • (1999) Biochemistry , vol.38 , Issue.48 , pp. 15994-16000
    • Rosenberg, C.1    Christian, J.2    Bricker, T.M.3    Putnam-Evans, C.4
  • 291
    • 67650033429 scopus 로고    scopus 로고
    • Effect of a single-amino acid substitution of the 43 kDa chlorophyll protein on the oxygen-evolving reaction of the cyanobacterium Synechocystis sp. PCC 6803: Analysis of the Glu354Gln mutation
    • Y. Shimada, H. Suzuki, T. Tsuchiya, T. Tomo, T. Noguchi and M. Mimuro: Effect of a Single-Amino Acid Substitution of the 43 kDa Chlorophyll Protein on the Oxygen-Evolving Reaction of the Cyanobacterium Synechocystis sp. PCC 6803: Analysis of the Glu354Gln Mutation. Biochemistry 48, 6095-6103 (2009)
    • (2009) Biochemistry , vol.48 , pp. 6095-6103
    • Shimada, Y.1    Suzuki, H.2    Tsuchiya, T.3    Tomo, T.4    Noguchi, T.5    Mimuro, M.6
  • 292
    • 57849114287 scopus 로고    scopus 로고
    • Uncovering channels in photosystem II by computer modelling: Current progress, future prospects, and lessons from analogous systems
    • DOI 10.1007/s11120-008-9358-2
    • F. Ho: Uncovering channels in photosystem II by computer modelling: current progress, future prospects, and lessons from analogous systems. Photosynth Res 98, 503-522 (2008) (Pubitemid 50274589)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 503-522
    • Ho, F.M.1
  • 293
    • 0001477239 scopus 로고
    • 2 accessibility to the photosystem II donor side in protein-depleted inside-out thylakoids measured as flash-induced oxygen production
    • 2 Accessibility to the Photosystem II Donor Side in Protein-Depleted inside-out Thylakoids Measured as Flash-Induced Oxygen Production. Biochim Biophys Acta 848, 359-363 (1986)
    • (1986) Biochim Biophys Acta , vol.848 , pp. 359-363
    • Schröder, W.P.1    Akerlund, H.E.2
  • 294
    • 0026743378 scopus 로고
    • The oxygen-evolving complex requires chloride to prevent hydrogen peroxide formation
    • DOI 10.1021/bi00163a033
    • P. L. Fine and W. D. Frasch: The Oxygen-Evolving Complex Requires Chloride to Prevent Hydrogen-Peroxide Formation. Biochemistry 31, 12204-12210 (1992) (Pubitemid 23011368)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 12204-12210
    • Fine, P.L.1    Frasch, W.D.2
  • 295
    • 1042290468 scopus 로고    scopus 로고
    • Production of reactive oxygen species in chloride- and calcium-depleted photosystem II and their involvement in photoinhibition
    • DOI 10.1016/j.bbabio.2003.12.003
    • A. Arató, N. Bondarava and A. Krieger-Liszkay: Production of reactive oxygen species in chloride-and calcium-depleted photosystem II and their involvement in photoinhibition. Biochim Biophys Acta 1608, 171-180 (2004) (Pubitemid 38198261)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1608 , Issue.2-3 , pp. 171-180
    • Arato, A.1    Bondarava, N.2    Krieger-Liszkay, A.3
  • 297
    • 57849150806 scopus 로고    scopus 로고
    • Singlet oxygen production in photosystem II and related protection mechanism
    • DOI 10.1007/s11120-008-9349-3
    • A. Krieger-Liszkay, C. Fufezan and A. Trebst: Singlet oxygen production in photosystem II and related protection mechanism. Photosynth Res 98, 551-564 (2008) (Pubitemid 50266021)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 551-564
    • Krieger-Liszkay, A.1    Fufezan, C.2    Trebst, A.3
  • 298
    • 67649948825 scopus 로고    scopus 로고
    • Production of reactive oxygen species by photosystem II
    • P. Pospísil: Production of reactive oxygen species by photosystem II. Biochim Biophys Acta 1787, 1151-1160 (2009)
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1151-1160
    • Pospísil, P.1
  • 299
    • 0041851885 scopus 로고    scopus 로고
    • Photoinhibition - A historical perspective
    • DOI 10.1023/A:1024969518145
    • N. Adir, H. Zer, S. Shochat and I. Ohad: Photoinhibition - a historical perspective. Photosynth Res 76, 343-370 (2003) (Pubitemid 37065010)
    • (2003) Photosynthesis Research , vol.76 , Issue.1-3 , pp. 343-370
    • Adir, N.1    Zer, H.2    Shochat, S.3    Ohad, I.4
  • 300
    • 38049025214 scopus 로고    scopus 로고
    • Photoinhibition of Photosystem II and photodamage of the oxygen evolving manganese cluster
    • E. Tyystjärvi: Photoinhibition of Photosystem II and photodamage of the oxygen evolving manganese cluster. Coord Chem Rev 252, 361-376 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 361-376
    • Tyystjärvi, E.1
  • 302
    • 36849028349 scopus 로고    scopus 로고
    • Photoinhibition of photosynthetic electron transport
    • Ed G. Renger. RSC Publishing, Cambridge, U. K.
    • I. Vass and E. Aro: Photoinhibition of Photosynthetic Electron Transport. In: Primary Processes of Photosynthesis, Principles and Apparatus. Ed G. Renger. RSC Publishing, Cambridge, U. K., 1, 393-425 (2008)
    • (2008) Primary Processes of Photosynthesis, Principles and Apparatus , vol.1 , pp. 393-425
    • Vass, I.1    Aro, E.2
  • 303
    • 0030042115 scopus 로고    scopus 로고
    • On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism
    • T. Wydrzynski, W. Hillier and J. Messinger: On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism. Physiol Plant 96, 342-350 (1996)
    • (1996) Physiol Plant , vol.96 , pp. 342-350
    • Wydrzynski, T.1    Hillier, W.2    Messinger, J.3
  • 304
    • 0004585289 scopus 로고
    • 2-evolving site determined with water analogs
    • 2-Evolving Site Determined with Water Analogs. FEBS Lett 152, 39-43 (1983)
    • (1983) FEBS Lett , vol.152 , pp. 39-43
    • Radmer, R.1    Ollinger, O.2
  • 305
    • 0004626095 scopus 로고
    • Resolution of the paradox of ammonia and hydroxylamine as substrate-analogs for the water-oxidation reaction catalyzed by photosystem II
    • W. F. Beck and G. W. Brudvig: Resolution of the Paradox of Ammonia and Hydroxylamine as Substrate-Analogs for the Water-Oxidation Reaction Catalyzed by Photosystem II. J Am Chem Soc 110, 1517-1523 (1988)
    • (1988) J Am Chem Soc , vol.110 , pp. 1517-1523
    • Beck, W.F.1    Brudvig, G.W.2
  • 306
    • 0032583539 scopus 로고    scopus 로고
    • ESEEM studies of alcohol binding to the manganese cluster of the oxygen evolving complex of photosystem II
    • DOI 10.1021/ja982713b
    • D. A. Force, D. W. Randall, G. A. Lorigan, K. L. Clemens and R. D. Britt: ESEEM studies of alcohol binding to the manganese cluster of the oxygen evolving complex of Photosystem II. J Am Chem Soc 120, 13321-13333 (1998) (Pubitemid 29025195)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.51 , pp. 13321-13333
    • Force, D.A.1    Randall, D.W.2    Lorigan, G.A.3    Clemens, K.L.4    Britt, R.D.5
  • 307
    • 0035846819 scopus 로고    scopus 로고
    • Does functional photosytem II complex have an oxygen channel?
    • DOI 10.1016/S0014-5793(00)02358-9, PII S0014579300023589
    • J. M. Anderson: Does functional photosystem II complex have an oxygen channel? FEBS Lett 488, 1-4 (2001) (Pubitemid 32332795)
    • (2001) FEBS Letters , vol.488 , Issue.1-2 , pp. 1-4
    • Anderson, J.M.1
  • 309
    • 0028908351 scopus 로고
    • Charge recombination reactions in photosystem II. 1. Yields, recombination pathways, and kinetics of the primary pair
    • F. van Mieghem, K. Brettel, B. Hillmann, A. Kamlowski, A. W. Rutherford and E. Schlodder: Charge Recombination Reactions in Photosystem II. 1. Yields, Recombination Pathways, and Kinetics of the Primary Pair. Biochemistry 34, 4798-4813 (1995)
    • (1995) Biochemistry , vol.34 , pp. 4798-4813
    • Van Mieghem, F.1    Brettel, K.2    Hillmann, B.3    Kamlowski, A.4    Rutherford, A.W.5    Schlodder, E.6
  • 310
    • 0036809979 scopus 로고    scopus 로고
    • Dual role of triplet localization on the accessory chlorophyll in the photosystem II reaction center: Photoprotection and photodamage of the D1 protein
    • T. Noguchi: Dual role of triplet localization on the accessory chlorophyll in the photosystem II reaction center: Photoprotection and photodamage of the D1 protein. Plant Cell Physiol 43, 1112-1116 (2002) (Pubitemid 35337206)
    • (2002) Plant and Cell Physiology , vol.43 , Issue.10 , pp. 1112-1116
    • Noguchi, T.1
  • 311
    • 0038322621 scopus 로고    scopus 로고
    • Physical mechanisms of generation and deactivation of singlet oxygen
    • C. Schweitzer and R. Schmidt: Physical mechanisms of generation and deactivation of singlet oxygen. Chem Rev 103, 1685-1757 (2003)
    • (2003) Chem Rev , vol.103 , pp. 1685-1757
    • Schweitzer, C.1    Schmidt, R.2
  • 312
    • 3343026433 scopus 로고    scopus 로고
    • Detection of an intermediate of photosynthetic water oxidation
    • DOI 10.1038/nature02676
    • J. Clausen and W. Junge: Detection of an intermediate of photosynthetic water oxidation. Nature 430, 480-483 (2004) (Pubitemid 38987913)
    • (2004) Nature , vol.430 , Issue.6998 , pp. 480-483
    • Clausen, J.1    Junge, W.2
  • 313
    • 25644458333 scopus 로고    scopus 로고
    • 2 backpressure monitored by delayed chlorophyll fluorescence
    • DOI 10.1021/bi051183a
    • 2 backpressure monitored by delayed chlorophyll fluorescence. Biochemistry 44, 12775-12779 (2005) (Pubitemid 41379400)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12775-12779
    • Clausen, J.1    Junge, W.2    Dau, H.3    Haumann, M.4
  • 314
    • 33744979772 scopus 로고    scopus 로고
    • Photosynthetic oxygen production
    • W. Junge and J. Clausen: Photosynthetic oxygen production. Science 312, 1470 (2006)
    • (2006) Science , vol.312 , pp. 1470
    • Junge, W.1    Clausen, J.2
  • 315
    • 33744979772 scopus 로고    scopus 로고
    • Photosynthetic oxygen production - Response
    • J. E. Penner-Hahn and C. F. Yocum: Photosynthetic oxygen production - Response. Science 312, 1470-1471 (2006)
    • (2006) Science , vol.312 , pp. 1470-1471
    • Penner-Hahn, J.E.1    Yocum, C.F.2
  • 316
    • 33744992236 scopus 로고    scopus 로고
    • Photosynthetic oxygen production - Response
    • H. Dau and M. Haumann: Photosynthetic oxygen production - Response. Science 312, 1471-1472 (2006)
    • (2006) Science , vol.312 , pp. 1471-1472
    • Dau, H.1    Haumann, M.2
  • 317
    • 64349104744 scopus 로고    scopus 로고
    • Photosynthetic oxygen evolution is not reversed at high oxygen pressures: Mechanistic consequences for the water-oxidizing complex
    • D. R. J. Kolling, T. S. Brown, G. Ananyev and G. C. Dismukes: Photosynthetic Oxygen Evolution Is Not Reversed at High Oxygen Pressures: Mechanistic Consequences for the Water-Oxidizing Complex. Biochemistry 48, 1381-1389 (2009)
    • (2009) Biochemistry , vol.48 , pp. 1381-1389
    • Kolling, D.R.J.1    Brown, T.S.2    Ananyev, G.3    Dismukes, G.C.4
  • 318
    • 56249092462 scopus 로고    scopus 로고
    • Photosynthetic water oxidation at elevated dioxygen partial pressure monitored by time-resolved X-ray absorption measurements
    • M. Haumann, A. Grundmeier, I. Zaharieva and H. Dau: Photosynthetic water oxidation at elevated dioxygen partial pressure monitored by time-resolved X-ray absorption measurements. Proc Natl Acad Sci U S A 105, 17384-17389 (2008)
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17384-17389
    • Haumann, M.1    Grundmeier, A.2    Zaharieva, I.3    Dau, H.4
  • 319
    • 33748897143 scopus 로고    scopus 로고
    • Memoir on the decomposition of water and of the bodies that it holds in solution by means of galvanic electricity
    • C. J. T. de Grotthuss: Memoir on the decomposition of water and of the bodies that it holds in solution by means of galvanic electricity. Biochim. Biophys Acta 1757, 871-875 (2006)
    • (2006) Biochim. Biophys Acta , vol.1757 , pp. 871-875
    • De Grotthuss, C.J.T.1
  • 320
    • 33749043747 scopus 로고    scopus 로고
    • Et tu Grotthuss! and other unfinished stories
    • S. Cukierman: Et tu, Grotthuss! and other unfinished stories. Biochim Biophys Acta 1757, 876-885 (2006)
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 876-885
    • Cukierman, S.1
  • 321
    • 33746601087 scopus 로고    scopus 로고
    • Design principles of proton-pumping haem-copper oxidases
    • DOI 10.1016/j.sbi.2006.06.012, PII S0959440X06001163
    • P. Brzezinski and P. Adelroth: Design principles of proton-pumping haem-copper oxidases. Curr Opin Struct Biol 16, 465-472 (2006) (Pubitemid 44149073)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.4 , pp. 465-472
    • Brzezinski, P.1    Adelroth, P.2
  • 322
    • 33749052047 scopus 로고    scopus 로고
    • Chance and design-Proton transfer in water, channels and bioenergetic proteins
    • DOI 10.1016/j.bbabio.2006.06.017, PII S0005272806001885
    • C. A. Wraight: Chance and design - Proton transfer in water, channels and bioenergetic proteins. Biochim Biophys Acta 1757, 886-912 (2006) (Pubitemid 44462697)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 886-912
    • Wraight, C.A.1
  • 323
    • 33646365537 scopus 로고    scopus 로고
    • Intraprotein proton transfer - Concepts and realities from the bacterial photosynthetic reaction center
    • Ed M. Wikstrom. RSC Publishing, Cambridge, UK
    • C. A. Wraight: Intraprotein Proton Transfer - Concepts and Realities from the Bacterial Photosynthetic Reaction Center. In: Biophysical and Structural Aspects of Bioenergetics. Ed M. Wikstrom. RSC Publishing, Cambridge, UK, 273-312 (2005)
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 273-312
    • Wraight, C.A.1
  • 324
    • 33144471312 scopus 로고    scopus 로고
    • Energetics of a possible proton exit pathway for water oxidation in photosystem II
    • DOI 10.1021/bi051615h
    • H. Ishikita, W. Saenger, B. Loll, J. Biesiadka and E. W. Knapp: Energetics of a possible proton exit pathway for water oxidation in photosystem II. Biochemistry 45, 2063-2071 (2006) (Pubitemid 43271306)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2063-2071
    • Ishikita, H.1    Saenger, W.2    Loll, B.3    Biesiadka, J.4    Knapp, E.-W.5
  • 325
    • 34547116864 scopus 로고    scopus 로고
    • Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel
    • DOI 10.1016/j.jsb.2007.01.016, PII S1047847707000238
    • J. W. Murray and J. Barber: Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel. J Struct Biol 159, 228-237 (2007) (Pubitemid 47096868)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 SPEC. ISSUE , pp. 228-237
    • Murray, J.W.1    Barber, J.2
  • 326
    • 38849188029 scopus 로고    scopus 로고
    • 4 cluster in Photosystem II based on solvent accessibility simulations, with implications for substrate water access
    • DOI 10.1016/j.bbabio.2007.08.009, PII S0005272807002009
    • F. M. Ho and S. Styring: Access channels and methanol binding site to the CaMn4 cluster in Photosystem II based on solvent accessibility simulations, with implications for substrate water access. Biochim Biophys Acta 1777, 140-153 (2008) (Pubitemid 351187745)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.2 , pp. 140-153
    • Ho, F.M.1    Styring, S.2
  • 327
    • 77749255459 scopus 로고    scopus 로고
    • Tracking the flow of water through photosystem ii using molecular dynamics and streamline tracing
    • S. Vassiliev, P. Comte, A. Mahboob and D. Bruce: Tracking the Flow of Water through Photosystem II Using Molecular Dynamics and Streamline Tracing. Biochemistry 49, 1873-1881 (2010)
    • (2010) Biochemistry , vol.49 , pp. 1873-1881
    • Vassiliev, S.1    Comte, P.2    Mahboob, A.3    Bruce, D.4
  • 329
    • 34147161261 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics structural models of the oxygen-evolving complex of photosystem II
    • DOI 10.1016/j.sbi.2007.03.015, PII S0959440X07000450, Theory and Simulation / Mecromolecular Assemblages
    • E. M. Sproviero, J. A. Gascon, J. P. McEvoy, G. W. Brudvig and V. S. Batista: Quantum mechanics/molecular mechanics structural models of the oxygen-evolving complex of photosystem II. Curr Opin Struct Biol 17, 173-180 (2007) (Pubitemid 46575260)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.2 , pp. 173-180
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 330
    • 0036869232 scopus 로고    scopus 로고
    • Diffusion-tensor MRI: Theory, experimental design and data analysis - A technical review
    • DOI 10.1002/nbm.783
    • P. J. Basser and D. K. Jones: Diffusion-tensor MRI: theory, experimental design and data analysis - a technical review. NMR Biomed 15, 456-467 (2002) (Pubitemid 36054509)
    • (2002) NMR in Biomedicine , vol.15 , Issue.7-8 , pp. 456-467
    • Basser, P.J.1    Jones, D.K.2
  • 331
    • 57849169340 scopus 로고    scopus 로고
    • Analysis of xenon binding to photosystem II by X-ray crystallography
    • DOI 10.1007/s11120-008-9366-2
    • J. W. Murray, K. Maghlaoui, J. Kargul, M. Sugiura and J. Barber: Analysis of xenon binding to photosystem II by X-ray crystallography. Photosynth Res 98, 523-527 (2008) (Pubitemid 50294457)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 523-527
    • Murray, J.W.1    Maghlaoui, K.2    Kargul, J.3    Sugiura, M.4    Barber, J.5
  • 333
    • 0034730423 scopus 로고    scopus 로고
    • Size versus polarizability in protein-ligand interactions: Binding of noble gases within engineered cavities in phage T4 lysozyme
    • M. L. Quillin, W. A. Breyer, I. J. Griswold and B. W. Matthews: Size versus polarizability in protein-ligand interactions: Binding of noble gases within engineered cavities in phage T4 lysozyme. J Mol Biol 302, 955-977 (2000)
    • (2000) J Mol Biol , vol.302 , pp. 955-977
    • Quillin, M.L.1    Breyer, W.A.2    Griswold, I.J.3    Matthews, B.W.4
  • 335
    • 42349083650 scopus 로고    scopus 로고
    • 3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • DOI 10.1021/bi800045y
    • 3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases. Biochemistry 47, 4657-4665 (2008) (Pubitemid 351555486)
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2    Fee, J.A.3    Stout, C.D.4
  • 336
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • A. Bondi: van der Waals Volumes and Radii. J Phys Chem 68, 441-451 (1964)
    • (1964) J Phys Chem , vol.68 , pp. 441-451
    • Bondi, A.1
  • 337
    • 0001421044 scopus 로고
    • The refractive indices and verdet constants of the inert gases
    • A. Dalgarno and A. E. Kingston: The Refractive Indices and Verdet Constants of the Inert Gases. Proc R Soc A 259, 424-431 (1960)
    • (1960) Proc R Soc A , vol.259 , pp. 424-431
    • Dalgarno, A.1    Kingston, A.E.2
  • 338
    • 36849140881 scopus 로고
    • Absolute determination of refractive indices of gases at 47.7 gigahertz
    • A. C. Newell and R. C. Baird: Absolute Determination of Refractive Indices of Gases at 47.7 Gigahertz. J Appl Phys 36, 3751-3759 (1965)
    • (1965) J Appl Phys , vol.36 , pp. 3751-3759
    • Newell, A.C.1    Baird, R.C.2
  • 340
    • 0002564682 scopus 로고
    • Chloride binding proteins: Mechanistic implications for the oxygen-evolving complex of photosystem II
    • W. J. Coleman: Chloride Binding Proteins: Mechanistic Implications for the Oxygen-Evolving Complex of Photosystem II. Photosynth Res 23, 1-27 (1990)
    • (1990) Photosynth Res , vol.23 , pp. 1-27
    • Coleman, W.J.1
  • 341
    • 4644351484 scopus 로고
    • 2 evolving enzyme in photosynthetic systems
    • 2 Evolving Enzyme in Photosynthetic Systems. FEBS Lett 177, 2-5 (1984)
    • (1984) FEBS Lett , vol.177 , pp. 2-5
    • Critchley, C.1    Sargeson, A.M.2
  • 342
    • 0001297780 scopus 로고
    • The chloride requirement for photosynthetic oxygen evolution - Analysis of the effects of chloride and other anions on amine inhibition of the oxygen-evolving complex
    • P. O. Sandusky and C. F. Yocum: The Chloride Requirement for Photosynthetic Oxygen Evolution - Analysis of the Effects of Chloride and Other Anions on Amine Inhibition of the Oxygen-Evolving Complex. Biochim Biophys Acta 766, 603-611 (1984)
    • (1984) Biochim Biophys Acta , vol.766 , pp. 603-611
    • Sandusky, P.O.1    Yocum, C.F.2
  • 343
    • 0023047350 scopus 로고
    • - reconstitution on the oxygenevolution rate, the yield of the multiline manganese EPR signal and EPR signal II in the isolated Photosystem-II complex
    • - reconstitution on the oxygenevolution rate, the yield of the multiline manganese EPR signal and EPR signal II in the isolated Photosystem-II complex. Biochim Biophys Acta 848, 378-391 (1986)
    • (1986) Biochim Biophys Acta , vol.848 , pp. 378-391
    • Damoder, R.1    Klimov, V.V.2    Dismukes, G.C.3
  • 345
    • 77953811966 scopus 로고    scopus 로고
    • Substitution of chloride by bromide modifies the low-temperature tyrosine Z oxidation in active photosystem II
    • Y. A. Ren, C. X. Zhang and J. Q. Zhao: Substitution of chloride by bromide modifies the low-temperature tyrosine Z oxidation in active photosystem II. Biochim Biophys Acta 1797, 1421-1427 (2010)
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1421-1427
    • Ren, Y.A.1    Zhang, C.X.2    Zhao, J.Q.3
  • 347
    • 66649106614 scopus 로고    scopus 로고
    • Location of chloride and its possible functions in oxygenevolving photosystem II revealed by X-ray crystallography
    • K. Kawakami, Y. Umena, N. Kamiya and J. R. Shen: Location of chloride and its possible functions in oxygenevolving photosystem II revealed by X-ray crystallography. Proc Natl Acad Sci U S A 106, 8567-8572 (2009)
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8567-8572
    • Kawakami, K.1    Umena, Y.2    Kamiya, N.3    Shen, J.R.4
  • 348
    • 0000474214 scopus 로고
    • The association of functional anions with the oxygen-evolving center of chloroplasts
    • P. H. Homann: The Association of Functional Anions with the Oxygen-Evolving Center of Chloroplasts. Biochim Biophys Acta 809, 311-319 (1985)
    • (1985) Biochim Biophys Acta , vol.809 , pp. 311-319
    • Homann, P.H.1
  • 349
    • 0000222974 scopus 로고
    • A model for the mechanism of chloride activation of oxygen evolution in photosystem II
    • W. J. Coleman and Govindjee: A Model for the Mechanism of Chloride Activation of Oxygen Evolution in Photosystem II. Photosynth Res 13, 199-223 (1987)
    • (1987) Photosynth Res , vol.13 , pp. 199-223
    • Coleman, W.J.1    Govindjee2
  • 350
    • 0037465425 scopus 로고    scopus 로고
    • The function of the chloride ion in photosynthetic oxygen evolution
    • DOI 10.1021/bi026175y
    • K. Olesen and L. E. Andréasson: The function of the chloride ion in photosynthetic oxygen evolution. Biochemistry 42, 2025-2035 (2003) (Pubitemid 36258676)
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 2025-2035
    • Olesen, K.1    Andreasson, L.-E.2
  • 351
    • 0002266330 scopus 로고
    • Is there a direct chloride cofactor requirement in the oxygen-evolving reactions of photosystem II
    • T. Wydrzynski, F. Baumgart, F. Macmillan and G. Renger: Is There a Direct Chloride Cofactor Requirement in the Oxygen-Evolving Reactions of Photosystem II. Photosynth Res 25, 59-72 (1990)
    • (1990) Photosynth Res , vol.25 , pp. 59-72
    • Wydrzynski, T.1    Baumgart, F.2    MacMillan, F.3    Renger, G.4
  • 353
    • 0000535040 scopus 로고
    • Studies of the slowly exchanging chloride in photosystem ii of higher plants
    • K. Lindberg, T. Vanngard and L. E. Andréasson: Studies of the Slowly Exchanging Chloride in Photosystem II of Higher Plants. Photosynth Res 38, 401-408 (1993)
    • (1993) Photosynth Res , vol.38 , pp. 401-408
    • Lindberg, K.1    Vanngard, T.2    Andréasson, L.E.3
  • 354
    • 0029805939 scopus 로고    scopus 로고
    • A one-site, two-state model for the binding of anions in photosystem II
    • DOI 10.1021/bi961244s
    • K. Lindberg and L. E. Andréasson: A one-site, twostate model for the binding of anions in photosystem II. Biochemistry 35, 14259-14267 (1996) (Pubitemid 26384421)
    • (1996) Biochemistry , vol.35 , Issue.45 , pp. 14259-14267
    • Lindberg, K.1    Andreasson, L.-E.2
  • 355
    • 0030025491 scopus 로고    scopus 로고
    • Properties of the chloride-depleted oxygen-evolving complex of photosystem II studied by electron paramagnetic resonance
    • DOI 10.1021/bi9514471
    • P. van Vliet and A. W. Rutherford: Properties of the chloride-depleted oxygen-evolving complex of photosystem II studied by electron paramagnetic resonance. Biochemistry 35, 1829-1839 (1996) (Pubitemid 26062632)
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 1829-1839
    • Van Vliet, P.1    Rutherford, A.W.2
  • 356
    • 0001117883 scopus 로고
    • 2-evolving complex? Studies of the substructure of the low-temperature multiline EPR Signal
    • 2-Evolving Complex? Studies of the Substructure of the Low-Temperature Multiline EPR Signal. Biochim Biophys Acta 850, 333-342 (1986)
    • (1986) Biochim Biophys Acta , vol.850 , pp. 333-342
    • Yachandra, V.K.1    Guiles, R.D.2    Sauer, K.3    Klein, M.P.4
  • 357
    • 0021377622 scopus 로고
    • Nonequilibration of membrane-associated protons with the internal aqueous space in dark-maintained chloroplast thylakoids
    • J. A. Laszlo, G. M. Baker and R. A. Dilley: Nonequilibration of Membrane-Associated Protons with the Internal Aqueous Space in Dark-Maintained Chloroplast Thylakoids. J Bioenerg Biomembr 16, 37-51 (1984)
    • (1984) J Bioenerg Biomembr , vol.16 , pp. 37-51
    • Laszlo, J.A.1    Baker, G.M.2    Dilley, R.A.3
  • 358
    • 0013447274 scopus 로고
    • Chloroplast thylakoid membrane proteins having buried amine buffering groups
    • J. A. Laszlo, G. M. Baker and R. A. Dilley: Chloroplast Thylakoid Membrane Proteins Having Buried Amine Buffering Groups. Biochim Biophys Acta 764, 160-169 (1984)
    • (1984) Biochim Biophys Acta , vol.764 , pp. 160-169
    • Laszlo, J.A.1    Baker, G.M.2    Dilley, R.A.3
  • 359
    • 0024712222 scopus 로고
    • Chloroplast thylakoid proteins associated with sequestered proton-buffering domains. Plastocyanin contributes buffering groups to localized proton domains
    • F. C. T. Allnutt, E. Atta-Asafo-Adjei and R. A. Dilley: Chloroplast Thylakoid Proteins Associated with Sequestered Proton-Buffering Domains. Plastocyanin Contributes Buffering Groups to Localized Proton Domains. J Bioenerg Biomembr 21, 535-551 (1989)
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 535-551
    • Allnutt, F.C.T.1    Atta-Asafo-Adjei, E.2    Dilley, R.A.3
  • 360
    • 45149089916 scopus 로고    scopus 로고
    • Biosynthetic exchange of bromide for chloride and strontium for calcium in the photosystem II oxygen-evolving enzymes
    • N. Ishida, M. Sugiura, F. Rappaport, T. L. Lai, A. W. Rutherford and A. Boussac: Biosynthetic exchange of bromide for chloride and strontium for calcium in the photosystem II oxygen-evolving enzymes. J Biol Chem 283, 13330-13340 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 13330-13340
    • Ishida, N.1    Sugiura, M.2    Rappaport, F.3    Lai, T.L.4    Rutherford, A.W.5    Boussac, A.6
  • 362
    • 0016433801 scopus 로고
    • The rapid component of electron paramagnetic resonance signal II: A candidate for the physiological donor to photosystem II in spinach chloroplasts
    • G. T. Babcock and K. Sauer: The rapid component of electron paramagnetic resonance signal II: a candidate for the physiological donor to photosystem II in spinach chloroplasts. Biochim Biophys Acta 376, 329-44 (1975)
    • (1975) Biochim Biophys Acta , vol.376 , pp. 329-344
    • Babcock, G.T.1    Sauer, K.2
  • 365
    • 0024976548 scopus 로고
    • Directed alteration of the D1 polypeptide of photosystem II: Evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680
    • J. G. Metz, P. J. Nixon, M. Rögner, G. W. Brudvig and B. A. Diner: Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry 28, 6960-9 (1989)
    • (1989) Biochemistry , vol.28 , pp. 6960-6969
    • Metz, J.G.1    Nixon, P.J.2    Rögner, M.3    Brudvig, G.W.4    Diner, B.A.5
  • 366
    • 0023781850 scopus 로고
    • Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system
    • R. J. Debus, B. A. Barry, G. T. Babcock and L. McIntosh: Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system. Proc Natl Acad Sci U S A 85, 427-430 (1988)
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 427-430
    • Debus, R.J.1    Barry, B.A.2    Babcock, G.T.3    McIntosh, L.4
  • 367
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • DOI 10.1126/science.277.5334.1953
    • C. W. Hoganson and G. T. Babcock: A metalloradical mechanism for the generation of oxygen from water in photosynthesis. Science 277, 1953-1956 (1997) (Pubitemid 27449129)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 368
    • 0032570284 scopus 로고    scopus 로고
    • Function of tyrosine Z in water oxidation by photosystem II: Electrostatical promotor instead of hydrogen abstractor
    • DOI 10.1021/bi9719152
    • R. Ahlbrink, M. Haumann, D. Cherepanov, O. Bögershausen, A. Mulkidjanian and W. Junge: Function of tyrosine Z in water oxidation by photosystem II: electrostatical promotor instead of hydrogen abstractor. Biochemistry 37, 1131-1142 (1998) (Pubitemid 28100616)
    • (1998) Biochemistry , vol.37 , Issue.4 , pp. 1131-1142
    • Ahlbrink, R.1    Haumann, M.2    Cherepanov, D.3    Bogershausen, O.4    Mulkidjanian, A.5    Junge, W.6
  • 369
    • 0032910389 scopus 로고    scopus 로고
    • Evidence for impaired hydrogen-bonding of tyrosine Y(Z) in calcium-depleted Photosystem II
    • DOI 10.1016/S0005-2728(99)00045-6, PII S0005272899000456
    • M. Haumann and W. Junge: Evidence for impaired hydrogen-bonding of tyrosine YZ in calcium-depleted photosystem II. Biochim Biophys Acta 1411, 121-133 (1999) (Pubitemid 29182802)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.1 , pp. 121-133
    • Haumann, M.1    Junge, W.2
  • 370
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • DOI 10.1016/S0005-2728(00)00069-4, PII S0005272800000694
    • C. Tommos and G. T. Babcock: Proton and hydrogen currents in photosynthetic water oxidation. Biochim Biophys Acta 1458, 199-219 (2000) (Pubitemid 30254260)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 371
    • 0035808688 scopus 로고    scopus 로고
    • Coupling of electron and proton transfer in the photosynthetic water oxidase
    • F. Rappaport and J. Lavergne: Coupling of electron and proton transfer in the photosynthetic water oxidase. Biochim Biophys Acta 1503, 246-259 (2001)
    • (2001) Biochim Biophys Acta , vol.1503 , pp. 246-259
    • Rappaport, F.1    Lavergne, J.2
  • 372
    • 37049097460 scopus 로고
    • The construction and use of potential-pH diagrams in organic oxidation-reduction reactions
    • S. I. Bailey, I. M. Ritchie and F. R. Hewgill: The Construction and Use of Potential-pH Diagrams in Organic Oxidation-Reduction Reactions. J Chem Soc Perkin Trans 2 645-652 (1983)
    • (1983) J Chem Soc Perkin Trans , vol.2 , pp. 645-652
    • Bailey, S.I.1    Ritchie, I.M.2    Hewgill, F.R.3
  • 374
    • 33748716572 scopus 로고
    • Determination of acidity constants of some phenol radical cations by means of electron spin resonance
    • W. T. Dixon and D. Murphy: Determination of Acidity Constants of Some Phenol Radical Cations by Means of Electron Spin Resonance. J Chem Soc Faraday Trans II 72, 1221-1230 (1976)
    • (1976) J Chem Soc Faraday Trans II , vol.72 , pp. 1221-1230
    • Dixon, W.T.1    Murphy, D.2
  • 375
    • 13844275382 scopus 로고    scopus 로고
    • Vibrational spectroscopy to study the properties of redox-active tyrosines in photosystem II and other proteins
    • DOI 10.1016/j.bbabio.2004.03.011
    • C. Berthomieu and R. Hienerwadel: Vibrational spectroscopy to study the properties of redox-active tyrosines in photosystem II and other proteins. Biochim Biophys Acta 1707, 51-66 (2005) (Pubitemid 40249941)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1707 , Issue.1 SPEC. ISSUE , pp. 51-66
    • Berthomieu, C.1    Hienerwadel, R.2
  • 376
    • 67849125417 scopus 로고    scopus 로고
    • Probing the coupling between proton and electron transfer in photosystem II core complexes containing a 3-fluorotyrosine
    • F. Rappaport, A. Boussac, D. A. Force, J. Peloquin, M. Brynda, M. Sugiura, S. Un, R. D. Britt and B. A. Diner: Probing the coupling between proton and electron transfer in photosystem II core complexes containing a 3-fluorotyrosine. J Am Chem Soc 131, 4425-4433 (2009)
    • (2009) J Am Chem Soc , vol.131 , pp. 4425-4433
    • Rappaport, F.1    Boussac, A.2    Force, D.A.3    Peloquin, J.4    Brynda, M.5    Sugiura, M.6    Un, S.7    Britt, R.D.8    Diner, B.A.9
  • 377
    • 32244442013 scopus 로고    scopus 로고
    • Mono-, di-, tri-, and tetra-substituted fluorotyrosines: New probes for enzymes that use tyrosyl radicals in catalysis
    • DOI 10.1021/ja055926r
    • M. R. Seyedsayamdost, S. Y. Reece, D. G. Nocera and J. Stubbe: Mono-, di-, tri-, and tetra-substituted fluorotyrosines: New probes for enzymes that use tyrosyl radicals in catalysis. J Am Chem Soc 128, 1569-1579 (2006) (Pubitemid 43214869)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.5 , pp. 1569-1579
    • Seyedsayamdost, M.R.1    Reece, S.Y.2    Nocera, D.G.3    Stubbe, J.4
  • 378
    • 33744918747 scopus 로고    scopus 로고
    • Function of redox-active tyrosine in photosystem II
    • DOI 10.1529/biophysj.105.076984
    • H. Ishikita and E. W. Knapp: Function of redox-active tyrosine in photosystem II. Biophys J 90, 3886-3896 (2006) (Pubitemid 43846107)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3886-3896
    • Ishikita, H.1    Knapp, E.-W.2
  • 379
    • 0026096798 scopus 로고
    • PH-dependent charge equilibria between tyrosine-D and the S-states in photosystem II. Estimation of relative midpoint redox potentials
    • I. Vass and S. Styring: pH-Dependent Charge Equilibria between Tyrosine-D and the S-States in Photosystem II. Estimation of Relative Midpoint Redox Potentials. Biochemistry 30, 830-839 (1991)
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 380
    • 34547893503 scopus 로고    scopus 로고
    • Oxidative photosynthetic water splitting: Energetics, kinetics and mechanism
    • DOI 10.1007/s11120-007-9185-x, Photosynthetic Water Oxidation
    • G. Renger: Oxidative photosynthetic water splitting: energetics, kinetics and mechanism. Photosynth Res 92, 407-425 (2007) (Pubitemid 47248573)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 407-425
    • Renger, G.1
  • 381
    • 34249805706 scopus 로고    scopus 로고
    • Reaction pattern and mechanism of light induced oxidative water splitting in photosynthesis
    • DOI 10.1016/j.bbabio.2006.12.004, PII S0005272806003707, Structure and Function of Photosystems
    • G. Renger and P. Kühn: Reaction pattern and mechanism of light induced oxidative water splitting in photosynthesis. Biochim Biophys Acta 1767, 458-471 (2007) (Pubitemid 46855728)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 458-471
    • Renger, G.1    Kuhn, P.2
  • 382
    • 0000385466 scopus 로고
    • 2-evolving PS II membrane fragments at different redox states si of the water oxidizing system
    • 2-Evolving PS II Membrane Fragments at Different Redox States Si of the Water Oxidizing System. FEBS Lett 236, 425-431 (1988)
    • (1988) FEBS Lett , vol.236 , pp. 425-431
    • Eckert, H.J.1    Renger, G.2
  • 384
    • 0032508393 scopus 로고    scopus 로고
    • Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study
    • DOI 10.1021/bi980510u
    • A. M. A. Hays, I. R. Vassiliev, J. H. Golbeck and R. J. Debus: Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study. Biochemistry 37, 11352-11365 (1998) (Pubitemid 28394885)
    • (1998) Biochemistry , vol.37 , Issue.32 , pp. 11352-11365
    • Hays, A.-M.A.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 385
    • 0039776010 scopus 로고    scopus 로고
    • Role of D1-His190 in the proton-coupled oxidation of tyrosine YZ in manganese-depleted photosystem II
    • A. M. A. Hays, I. R. Vassiliev, J. H. Golbeck and R. J. Debus: Role of D1-His190 in the proton-coupled oxidation of tyrosine YZ in manganese-depleted photosystem II. Biochemistry 38, 11851-1185 (1999)
    • (1999) Biochemistry , vol.38 , pp. 11851-11185
    • Hays, A.M.A.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 386
    • 8144219977 scopus 로고    scopus 로고
    • +· reduction pattern and its temperature dependence in oxygen-evolving PSII core complexes from a thermophilic cyanobacteria and higher plants
    • +· reduction pattern and its temperature dependence in oxygen-evolving PSII core complexes from a thermophilic cyanobacteria and higher plants. Phys Chem Chem Phys 6, 4838-4843 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4838-4843
    • Kühn, P.1    Eckert, H.2    Eichler, H.J.3    Renger, G.4
  • 387
    • 0030046368 scopus 로고    scopus 로고
    • Effects of hydrogen/deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach
    • DOI 10.1016/0014-5793(95)01433-0
    • M. Karge, K. D. Irrgang, S. Sellin, R. Feinäugle, B. Liu, H. J. Eckert, H. J. Eichler and G. Renger: Effects of hydrogen/deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach. FEBS Lett 378, 140-144 (1996) (Pubitemid 26015561)
    • (1996) FEBS Letters , vol.378 , Issue.2 , pp. 140-144
    • Karge, M.1    Irrgang, K.-D.2    Sellin, S.3    Feinaugle, R.4    Liu, B.5    Eckert, H.-J.6    Eichler, H.J.7    Renger, G.8
  • 388
    • 0030970415 scopus 로고    scopus 로고
    • Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of photosystem II
    • DOI 10.1023/A:1005861917596
    • M. Haumann, O. Bögershausen, D. Cherepanov, R. Ahlbrink and W. Junge: Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of Photosystem II. Photosynth Res 51, 193-208 (1997) (Pubitemid 27275238)
    • (1997) Photosynthesis Research , vol.51 , Issue.3 , pp. 193-208
    • Haumann, M.1    Bogershausen, O.2    Cherepanov, D.3    Ahlbrink, R.4    Junge, W.5
  • 389
    • 0033573843 scopus 로고    scopus 로고
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects. Biochemistry 38, 2068-2077 (1999)
    • (1999) Biochemistry , vol.38 , pp. 2068-2077
    • Christen, G.1    Renger, G.2
  • 391
    • 0033545726 scopus 로고    scopus 로고
    • +· reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids
    • +· reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids. Biochemistry 38, 6082-6092 (1999)
    • (1999) Biochemistry , vol.38 , pp. 6082-6092
    • Christen, G.1    Seeliger, A.2    Renger, G.3
  • 392
  • 393
    • 18244404033 scopus 로고    scopus 로고
    • Trapping of metalloradical intermediates of the S-states at liquid helium temperatures. Overview of the phenomenology and mechanistic implications
    • DOI 10.1021/bi0503201
    • V. Petrouleas, D. Koulougliotis and N. Ioannidis: Trapping of metalloradical intermediates of the S-states at liquid helium temperatures. Overview of the phenomenology and mechanistic implications. Biochemistry 44, 6723-6728 (2005) (Pubitemid 40632391)
    • (2005) Biochemistry , vol.44 , Issue.18 , pp. 6723-6728
    • Petrouleas, V.1    Koulougliotis, D.2    Ioannidis, N.3
  • 395
    • 0001404648 scopus 로고
    • Deactivation kinetics and temperature-dependence of the S-state transitions in the oxygen-evolving system of photosystem II measured by EPR spectroscopy
    • S. Styring and A. W. Rutherford: Deactivation Kinetics and Temperature-Dependence of the S-State Transitions in the Oxygen-Evolving System of Photosystem II Measured by EPR Spectroscopy. Biochim Biophys Acta 933, 378-387 (1988)
    • (1988) Biochim Biophys Acta , vol.933 , pp. 378-387
    • Styring, S.1    Rutherford, A.W.2
  • 396
    • 7244240549 scopus 로고    scopus 로고
    • Low-temperature electron transfer in photosystem II: A tyrosyl radical and semiquinone charge pair
    • DOI 10.1021/bi048631j
    • C. X. Zhang, A. Boussac and A. W. Rutherford: Lowtemperature electron transfer in photosystem II: A tyrosyl radical and semiquinone charge pair. Biochemistry 43, 13787-13795 (2004) (Pubitemid 39431062)
    • (2004) Biochemistry , vol.43 , Issue.43 , pp. 13787-13795
    • Zhang, C.1    Boussac, A.2    Rutherford, A.W.3
  • 397
    • 33646877236 scopus 로고    scopus 로고
    • 3 state intermediate of the oxygen-evolving complex of photosystem II
    • DOI 10.1021/bi060520s
    • 3 state intermediate of the oxygen-evolving complex of photosystem II. Biochemistry 45, 6252-6259 (2006) (Pubitemid 43787792)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6252-6259
    • Ioannidis, N.1    Zahariou, G.2    Petrouleas, V.3
  • 398
    • 0029941460 scopus 로고    scopus 로고
    • Conversion of the spin state of the manganese complex in photosystem II induced by near-infrared light
    • DOI 10.1021/bi960636w
    • A. Boussac, J. J. Girerd and A. W. Rutherford: Conversion of the spin state of the manganese complex in photosystem II induced by near-infrared light. Biochemistry 35, 6984-6989 (1996) (Pubitemid 26182086)
    • (1996) Biochemistry , vol.35 , Issue.22 , pp. 6984-6989
    • Boussac, A.1    Girerd, J.-J.2    Rutherford, A.W.3
  • 399
    • 0001260769 scopus 로고    scopus 로고
    • High-spin states (S > 5/2) of the photosystem II manganese complex
    • DOI 10.1021/bi9728710
    • A. Boussac, S. Un, O. Horner and A. W. Rutherford: High-spin states (S > 5/2) of the photosystem II manganese complex. Biochemistry 37, 4001-4007 (1998) (Pubitemid 28166421)
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4001-4007
    • Boussac, A.1    Un, S.2    Horner, O.3    Rutherford, A.W.4
  • 400
    • 0032560589 scopus 로고    scopus 로고
    • 2-state of the manganese complex of photosystem II from Synechococcus elongatus
    • DOI 10.1021/bi980195b
    • 2-state of the manganese complex of photosystem II from Synechococcus elongatus. Biochemistry 37, 8995-9000 (1998) (Pubitemid 28299669)
    • (1998) Biochemistry , vol.37 , Issue.25 , pp. 8995-9000
    • Boussac, A.1    Kuhl, H.2    Un, S.3    Rogner, M.4    Rutherford, A.W.5
  • 403
    • 0034649367 scopus 로고    scopus 로고
    • EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus
    • A. Boussac, M. Sugiura, Y. Inoue and A. W. Rutherford: EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus. Biochemistry 39, 13788-13799 (2000)
    • (2000) Biochemistry , vol.39 , pp. 13788-13799
    • Boussac, A.1    Sugiura, M.2    Inoue, Y.3    Rutherford, A.W.4
  • 405
    • 0037199463 scopus 로고    scopus 로고
    • 2 state configuration
    • DOI 10.1021/bi0159938
    • 2 state configuration. Biochemistry 41, 9580-9588 (2002) (Pubitemid 34810033)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9580-9588
    • Ioannidis, N.1    Petrouleas, V.2
  • 406
    • 0037199443 scopus 로고    scopus 로고
    • 3 state of the oxygen-evolving complex of photosystem II
    • DOI 10.1021/bi0159940
    • 3 state of the oxygen-evolving complex of photosystem II. Biochemistry 41, 9589-9600 (2002) (Pubitemid 34810034)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9589-9600
    • Ioannidis, N.1    Nugent, J.H.A.2    Petrouleas, V.3
  • 407
    • 70350140360 scopus 로고    scopus 로고
    • 0 state of the water oxidizing complex in photosystem II: PH dependence of the EPR split signal induction and mechanistic implications
    • 0 State of the Water Oxidizing Complex in Photosystem II: pH Dependence of the EPR Split Signal Induction and Mechanistic Implications. Biochemistry 48, 9393-9404 (2009)
    • (2009) Biochemistry , vol.48 , pp. 9393-9404
    • Sjöholm, J.1    Havelius, K.G.V.2    Mamedov, F.3    Styring, S.4
  • 408
    • 34347386893 scopus 로고    scopus 로고
    • D in photosystem II probed by illumination at 5 K
    • DOI 10.1021/bi700377g
    • D in photosystem II probed by illumination at 5 K. Biochemistry 46, 7865-7874 (2007) (Pubitemid 47018227)
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7865-7874
    • Havelius, K.G.V.1    Styring, S.2
  • 409
    • 13444301152 scopus 로고    scopus 로고
    • pH dependence of the flash-induced S-state transitions in the oxygen-evolving center of photosystem II from Thermosynechoccocus elongatus as revealed by fourier transform infrared spectroscopy
    • DOI 10.1021/bi0483312
    • H. Suzuki, M. Sugiura and T. Noguchi: pH dependence of the flash-induced S-state transitions in the oxygen-evolving center of photosystem II from Thermosynechoccocus elongatus as revealed by Fourier transform infrared spectroscopy. Biochemistry 44, 1708-1718 (2005) (Pubitemid 40204412)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1708-1718
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 411
    • 0001375803 scopus 로고
    • Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803 - Donor D is a tyrosine residue in the D2 protein
    • W. F. J. Vermaas, A. W. Rutherford and Ö. Hansson: Site-Directed Mutagenesis in Photosystem II of the Cyanobacterium Synechocystis sp. PCC 6803 - Donor D Is a Tyrosine Residue in the D2 Protein. Proc Natl Acad Sci U S A 85, 8477-8481 (1988)
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8477-8481
    • Vermaas, W.F.J.1    Rutherford, A.W.2    Hansson, O.3
  • 412
    • 0037154125 scopus 로고    scopus 로고
    • A functional role for tyrosine-D in assembly of the inorganic core of the water oxidase complex of photosystem II and the kinetics of water oxidation
    • DOI 10.1021/bi011528z
    • G. M. Ananyev, I. Sakiyan, B. A. Diner and G. C. Dismukes: A functional role for tyrosine-D in assembly of the inorganic core of the water oxidase complex of photosystem II and the kinetics of water oxidation. Biochemistry 41, 974-980 (2002) (Pubitemid 34062000)
    • (2002) Biochemistry , vol.41 , Issue.3 , pp. 974-980
    • Ananyev, G.M.1    Sakiyan, I.2    Diner, B.A.3    Dismukes, G.C.4
  • 413
    • 0025076277 scopus 로고
    • Electron-transfer reactions in manganese-depleted photosystem II
    • C. A. Buser, L. K. Thompson, B. A. Diner and G. W. Brudvig: Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry 29, 8977-8985 (1990) (Pubitemid 20311973)
    • (1990) Biochemistry , vol.29 , Issue.38 , pp. 8977-8985
    • Buser, C.A.1    Thompson, L.K.2    Diner, B.A.3    Brudvig, G.W.4
  • 415
    • 0037195238 scopus 로고    scopus 로고
    • Tyrosine D oxidation at cryogenic temperature in photosystem II
    • DOI 10.1021/bi026588z
    • P. Faller, A. W. Rutherford and R. J. Debus: Tyrosine D oxidation at cryogenic temperature in photosystem II. Biochemistry 41, 12914-12920 (2002) (Pubitemid 35215773)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12914-12920
    • Faller, P.1    Rutherford, A.W.2    Debus, R.J.3
  • 417
    • 0042666844 scopus 로고    scopus 로고
    • Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns
    • DOI 10.1021/bi034744b
    • S. Isgandarova, G. Renger and J. Messinger: Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns. Biochemistry 42, 8929-8938 (2003) (Pubitemid 36935400)
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 8929-8938
    • Isgandarova, S.1    Renger, G.2    Messinger, J.3
  • 418
    • 33746153380 scopus 로고    scopus 로고
    • Characterization of the water oxidizing complex of photosystem II of the Chl d-containing cyanobacterium Acaryochloris marina via its reactivity towards endogenous electron donors and acceptors
    • D. Shevela, B. Nöring, H. J. Eckert, J. Messinger and G. Renger: Characterization of the water oxidizing complex of photosystem II of the Chl d-containing cyanobacterium Acaryochloris marina via its reactivity towards endogenous electron donors and acceptors. Phys Chem Chem Phys 8, 3460-3466 (2006)
    • (2006) Phys Chem Chem Phys , vol.8 , pp. 3460-3466
    • Shevela, D.1    Nöring, B.2    Eckert, H.J.3    Messinger, J.4    Renger, G.5
  • 419
    • 0015760626 scopus 로고
    • Electron-paramagnetic resonance signal II in spinach chloroplasts. I. Kinetic-analysis for untreated chloroplasts
    • G. T. Babcock and K. Sauer: Electron-Paramagnetic Resonance Signal II in Spinach Chloroplasts. I. Kinetic-Analysis for Untreated Chloroplasts. Biochim Biophys Acta 325, 483-503 (1973)
    • (1973) Biochim Biophys Acta , vol.325 , pp. 483-503
    • Babcock, G.T.1    Sauer, K.2
  • 420
    • 48549111809 scopus 로고
    • Midpoint Potential of Signal II (Slow) in Tris-Washed Photosystem-II Particles
    • A. Boussac and A. L. Etienne: Midpoint Potential of Signal II (Slow) in Tris-Washed Photosystem-II Particles. Biochim Biophys Acta 766, 576-581 (1984)
    • (1984) Biochim Biophys Acta , vol.766 , pp. 576-581
    • Boussac, A.1    Etienne, A.L.2
  • 421
  • 422
    • 0027286757 scopus 로고
    • Modified EPR spectra of the tyrosine(D) radical in photosystem II in site- directed mutants of Synechocystis sp. PCC 6803: Identification of side chains in the immediate vicinity of tyrosine(D) on the D2 protein
    • C. Tommos, L. Davidsson, B. Svensson, C. Madsen, W. Vermaas and S. Styring: Modified EPR-Spectra of the TyrosineD Radical in Photosystem II in Site-Directed Mutants of Synechocystis sp. PCC 6803: Identification of Side Chains in the Immediate Vicinity of TyrosineD on the D2 Protein. Biochemistry 32, 5436-5441 (1993) (Pubitemid 23167986)
    • (1993) Biochemistry , vol.32 , Issue.20 , pp. 5436-5441
    • Tommos, C.1    Davidsson, L.2    Svensson, B.3    Madsen, C.4    Vermaas, W.5    Styring, S.6
  • 423
    • 0027762443 scopus 로고
    • Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center
    • DOI 10.1021/bi00212a045
    • X. S. Tang, D. A. Chisholm, G. C. Dismukes, G. W. Brudvig and B. A. Diner: Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center. Biochemistry 32, 13742-13748 (1993) (Pubitemid 24020254)
    • (1993) Biochemistry , vol.32 , Issue.49 , pp. 13742-13748
    • Tang, X.-S.1    Chisholm, D.A.2    Dismukes, G.C.3    Brudvig, G.W.4    Diner, B.A.5
  • 424
    • 0030041464 scopus 로고    scopus 로고
    • 245 GHz highfield EPR study of tyrosine-Do and tyrosine-Zo in mutants of photosystem II
    • S. Un, X. S. Tang and B. A. Diner: 245 GHz highfield EPR study of tyrosine-Do and tyrosine-Zo in mutants of photosystem II. Biochemistry 35, 679-684 (1996)
    • (1996) Biochemistry , vol.35 , pp. 679-684
    • Un, S.1    Tang, X.S.2    Diner, B.A.3
  • 427
    • 44649122732 scopus 로고    scopus 로고
    • Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II
    • R. Hienerwadel, B. A. Diner and C. Berthomieu: Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II. Biochim Biophys Acta 1777, 525-531 (2008)
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 525-531
    • Hienerwadel, R.1    Diner, B.A.2    Berthomieu, C.3
  • 428
    • 73249128237 scopus 로고    scopus 로고
    • A quantum mechanics/molecular mechanics study of the tyrosine residue, TyrD, of Photosystem II
    • R. Hart and P. J. O'Malley: A quantum mechanics/molecular mechanics study of the tyrosine residue, TyrD, of Photosystem II. Biochim Biophys Acta 1797, 250-254 (2010)
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 250-254
    • Hart, R.1    O'malley, P.J.2
  • 429
    • 0001740481 scopus 로고
    • Proton release during the redox cycle of the water oxidase
    • J. Lavergne and W. Junge: Proton Release during the Redox Cycle of the Water Oxidase. Photosynth Res 38, 279-296 (1993)
    • (1993) Photosynth Res , vol.38 , pp. 279-296
    • Lavergne, J.1    Junge, W.2
  • 431
    • 67650517036 scopus 로고    scopus 로고
    • Monitoring proton release during photosynthetic water oxidation in photosystem II by means of isotope-edited infrared spectroscopy
    • H. Suzuki, M. Sugiura and T. Noguchi: Monitoring Proton Release during Photosynthetic Water Oxidation in Photosystem II by Means of Isotope-Edited Infrared Spectroscopy. J Am Chem Soc 131, 7849-7857 (2009)
    • (2009) J Am Chem Soc , vol.131 , pp. 7849-7857
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 432
    • 0017703250 scopus 로고
    • Proton evolution from Photosystem II. Stoichiometry and mechanistic considerations
    • C. F. Fowler: Proton Evolution from Photosystem II Stoichiometry and Mechanistic Considerations. Biochim Biophys Acta 462, 414-421 (1977) (Pubitemid 8219391)
    • (1977) Biochimica et Biophysica Acta , vol.462 , Issue.2 , pp. 414-421
    • Fowler, C.F.1
  • 433
    • 0017395456 scopus 로고
    • Protolytic reactions in photosystem II: A new model for the release of protons accompanying the photooxidation of water
    • S. Saphon and A. R. Crofts: Protolytic Reactions in Photosystem II: A New Model for Release of Protons Accompanying Photooxidation of Water. Z Naturforsch C 32, 617-626 (1977) (Pubitemid 8165513)
    • (1977) Zeitschrift fur Naturforschung Section C Biosciences , vol.32 , Issue.7-8 , pp. 617-626
    • Saphon, S.1    Crofts, A.R.2
  • 434
    • 25544442100 scopus 로고
    • The role of pH and membrane potential in the reactions of photosystem II as measured by effects on delayed fluorescence
    • J. M. Bowes and A. R. Crofts: The Role of pH and Membrane Potential in the Reactions of Photosystem II as Measured by Effects on Delayed Fluorescence. Biochim Biophys Acta 637, 464-472 (1981)
    • (1981) Biochim Biophys Acta , vol.637 , pp. 464-472
    • Bowes, J.M.1    Crofts, A.R.2
  • 435
    • 13444289960 scopus 로고
    • Measurement of proton translocation in thylakoids under flashing light using a spin-labeled amine
    • B. Wille and J. Lavergne: Measurement of Proton Translocation in Thylakoids under Flashing Light Using a Spin-Labeled Amine. Photobiochem Photobiophys 4, 131-144 (1982)
    • (1982) Photobiochem Photobiophys , vol.4 , pp. 131-144
    • Wille, B.1    Lavergne, J.2
  • 436
    • 84989695074 scopus 로고
    • Stoichiometry and kinetics of proton release upon photosynthetic water oxidation
    • V. Förster and W. Junge: Stoichiometry and Kinetics of Proton
    • (1985) Photochem Photobiol , vol.41 , pp. 183-190
    • Förster, V.1    Junge, W.2
  • 437
    • 0026045872 scopus 로고
    • Proton release during successive oxidation steps of the photosynthetic water oxidation process - Stoichiometries and pH dependence
    • F. Rappaport and J. Lavergne: Proton Release during Successive Oxidation Steps of the Photosynthetic Water Oxidation Process - Stoichiometries and pH Dependence. Biochemistry 30, 10004-10012 (1991)
    • (1991) Biochemistry , vol.30 , pp. 10004-10012
    • Rappaport, F.1    Lavergne, J.2
  • 438
    • 0032741499 scopus 로고    scopus 로고
    • Stoichiometry of proton release from the catalytic center in photosynthetic water oxidation - Reexamination by a glass electrode study at pH 5.5-7.2
    • E. Schlodder and H. T. Witt: Stoichiometry of proton release from the catalytic center in photosynthetic water oxidation - Reexamination by a glass electrode study at pH 5.5-7.2. J Biol Chem 274, 30387-30392 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 30387-30392
    • Schlodder, E.1    Witt, H.T.2
  • 439
    • 79959548205 scopus 로고
    • Proton translocations in isolated spinach chloroplasts after single-turnover actinic flashes
    • A. B. Hope and A. Morland: Proton Translocations in Isolated Spinach Chloroplasts after Single-Turnover Actinic Flashes. Aust J Plant Physiol 6, 289-304 (1979)
    • (1979) Aust J Plant Physiol , vol.6 , pp. 289-304
    • Hope, A.B.1    Morland, A.2
  • 440
    • 0026665269 scopus 로고
    • Proton release during the four steps of photosynthetic water oxidation: Induction of 1:1:1:1 pattern due to lack of chlorophyll a/b binding proteins
    • P. Jahns and W. Junge: Proton release during the four steps of photosynthetic water oxidation: induction of 1:1:1:1 pattern due to lack of chlorophyll a/b binding proteins. Biochemistry 31, 7398-7403 (1992)
    • (1992) Biochemistry , vol.31 , pp. 7398-7403
    • Jahns, P.1    Junge, W.2
  • 441
    • 0027458064 scopus 로고
    • Photosynthetic water oxidation under flashing light. Oxygen release, proton release and absorption transients in the near ultraviolet - A comparison between thylakoids and a reaction-centre core preparation
    • DOI 10.1016/0005-2728(93)90021-7
    • K. Lübbers, M. Haumann and W. Junge: Photosynthetic Water Oxidation under Flashing Light. Oxygen Release, Proton Release and Absorption Transients in the near Ultraviolet - a Comparison between Thylakoids and a Reaction-Centre Core Preparation. Biochim Biophys Acta 1183, 210-214 (1993) (Pubitemid 23322971)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1183 , Issue.1 , pp. 210-214
    • Lubbers, K.1    Haumann, M.2    Junge, W.3
  • 442
    • 0343994244 scopus 로고
    • Investigation of pH-change-patterns of photosystem-II membrane fragments from spinach
    • Ed M. Baltscheffsky. Kluwer, Dordrecht
    • U. Wacker, E. Haag and G. Renger: Investigation of pH-change-patterns of photosystem-II membrane fragments from spinach. In: Current Research in Photosynthesis. Ed M. Baltscheffsky. Kluwer, Dordrecht, 1, 869-872 (1990)
    • (1990) Current Research in Photosynthesis , vol.1 , pp. 869-872
    • Wacker, U.1    Haag, E.2    Renger, G.3
  • 443
    • 8144230165 scopus 로고    scopus 로고
    • Structure-based mechanism of photosynthetic water oxidation
    • J. P. McEvoy and G. W. Brudvig: Structure-based mechanism of photosynthetic water oxidation. Phys Chem Chem Phys 6, 4754-4763 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4754-4763
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 444
    • 0033514442 scopus 로고    scopus 로고
    • Site-directed mutagenesis of basic arginine residues 305 and 342 in the CP 43 protein of photosystem II affects oxygen-evolving activity in Synechocystis 6803
    • N. Knoepfle, T. M. Bricker and C. Putnam-Evans: Site-directed mutagenesis of basic arginine residues 305 and 342 in the CP 43 protein of photosystem II affects oxygen-evolving activity in Synechocystis 6803. Biochemistry 38, 1582-1588 (1999)
    • (1999) Biochemistry , vol.38 , pp. 1582-1588
    • Knoepfle, N.1    Bricker, T.M.2    Putnam-Evans, C.3
  • 445
    • 29144513754 scopus 로고    scopus 로고
    • Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II
    • DOI 10.1039/b507519j
    • G. Ananyev, T. Nguyen, C. Putnam-Evans and G. C. Dismukes: Mutagenesis of CP43-arginine-357 to serine reveals new evidence for (bi)carbonate functioning in the water oxidizing complex of Photosystem II. Photochem Photobiol Sci 4, 991-998 (2005) (Pubitemid 41811361)
    • (2005) Photochemical and Photobiological Sciences , vol.4 , Issue.12 , pp. 991-998
    • Ananyev, G.1    Nguyen, T.2    Putnam-Evans, C.3    Dismukes, G.C.4
  • 446
    • 35649007241 scopus 로고    scopus 로고
    • 2O oxidation complex
    • DOI 10.1021/bi701387b
    • H. J. Hwang, P. Dilbeck, R. J. Debus and R. L. Burnap: Mutation of arginine 357 of the CP43 protein of photosystem II severely impairs the catalytic S-state cycle of the HiO oxidation complex. Biochemistry 46, 11987-11997 (2007) (Pubitemid 350022356)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 11987-11997
    • Hong, J.H.1    Dilbeck, P.2    Debus, R.J.3    Burnap, R.L.4
  • 447
    • 8144230689 scopus 로고    scopus 로고
    • Structural model of the oxygen-evolving centre of photosystem II with mechanistic implications
    • J. Barber, K. Ferreira, K. Maghlaoui and S. Iwata: Structural model of the oxygen-evolving centre of photosystem II with mechanistic implications. Phys Chem Chem Phys 6, 4737-4742 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4737-4742
    • Barber, J.1    Ferreira, K.2    Maghlaoui, K.3    Iwata, S.4
  • 448
    • 4043080672 scopus 로고    scopus 로고
    • Analysis of the structure of the PsbO protein and its implications
    • DOI 10.1023/B:PRES.0000036889.44048.e4
    • J. De Las Rivas and J. Barber: Analysis of the structure of the PsbO protein and its implications. Photosynth Res 81, 329-343 (2004) (Pubitemid 39059693)
    • (2004) Photosynthesis Research , vol.81 , Issue.3 , pp. 329-343
    • De Las Rivas, J.1    Barber, J.2
  • 449
    • 34249787880 scopus 로고    scopus 로고
    • A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II
    • DOI 10.1016/j.bbabio.2007.01.020, PII S0005272807000230, Structure and Function of Photosystems
    • T. Shutova, V. V. Klimov, B. Andersson and G. Samuelsson: A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II. Biochim Biophys Acta 1767, 434-440 (2007) (Pubitemid 46855746)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 434-440
    • Shutova, T.1    Klimov, V.V.2    Andersson, B.3    Samuelsson, G.4
  • 450
    • 77955262868 scopus 로고    scopus 로고
    • 4Ca Cluster of Photosystem II Involving D1-Glu65, D2-Glu312, and D1-Glu329
    • 4Ca Cluster of Photosystem II Involving D1-Glu65, D2-Glu312, and D1-Glu329. Biochemistry 49, 6655-6669 (2010)
    • (2010) Biochemistry , vol.49 , pp. 6655-6669
    • Service, R.J.1    Hillier, W.2    Debus, R.J.3
  • 451
    • 38049079870 scopus 로고    scopus 로고
    • 18O-Water exchange in photosystem II: Substrate binding and intermediates of the water splitting cycle
    • 18O-Water exchange in photosystem II: Substrate binding and intermediates of the water splitting cycle. Coord Chem Rev 252, 306-317 (2008)
    • (2008) Coord Chem Rev , vol.252 , pp. 306-317
    • Hillier, W.1    Wydrzynski, T.2
  • 452
    • 38949090403 scopus 로고    scopus 로고
    • FTIR detection of water reactions in the oxygen-evolving centre of photosystem II
    • T. Noguchi: FTIR detection of water reactions in the oxygen-evolving centre of photosystem II. Phil Trans R Soc B 363, 1189-1195 (2008)
    • (2008) Phil Trans R Soc B , vol.363 , pp. 1189-1195
    • Noguchi, T.1
  • 457
    • 33745019085 scopus 로고    scopus 로고
    • ESEEM studies of substrate water and small alcohol binding to the oxygen-evolving complex of photosystem II during functional turnover
    • DOI 10.1021/bi052146m
    • K. A. Ahrling, M. C. W. Evans, J. H. A. Nugent, R. J. Ball and R. J. Pace: ESEEM studies of substrate water and small alcohol binding to the oxygen-evolving complex of photosystem II during functional turnover. Biochemistry 45, 7069-7082 (2006) (Pubitemid 43877395)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7069-7082
    • Ahrling, K.A.1    Evans, M.C.W.2    Nugent, J.H.A.3    Ball, R.J.4    Pace, R.J.5
  • 458
    • 33947178988 scopus 로고    scopus 로고
    • Protons bound to the Mn cluster in photosystem II oxygen evolving complex detected by proton matrix ENDOR
    • DOI 10.1016/j.bbabio.2007.02.001, PII S0005272807000278
    • H. Yamada, H. Mino and S. Itoh: Protons bound to the Mn cluster in photosystem II oxygen evolving complex detected by proton matrix ENDOR. Biochim Biophys Acta 1767, 197-203 (2007) (Pubitemid 46400606)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.3 , pp. 197-203
    • Yamada, H.1    Mino, H.2    Itoh, S.3
  • 461
    • 0034681951 scopus 로고    scopus 로고
    • 2 evolving complex of photosystem II vary independently during S-state turnover
    • DOI 10.1021/bi992318d
    • 2 evolving complex of photosystem II vary independently during Sstate turnover. Biochemistry 39, 4399-4405 (2000) (Pubitemid 30212656)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4399-4405
    • Hillier, W.1    Wydrzynski, T.2
  • 462
    • 33746348022 scopus 로고    scopus 로고
    • Determination of μ-oxo exchange rates in di-μ-oxo dimanganese complexes by electrospray ionization mass spectrometry
    • DOI 10.1021/ja061348i
    • R. Tagore, H. Y. Chen, R. H. Crabtree and G. W. Brudvig: Determination of μ-oxo exchange rates in di-μ-oxo dimanganese complexes by electrospray ionization mass spectrometry. J Am Chem Soc 128, 9457-9465 (2006) (Pubitemid 44117106)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.29 , pp. 9457-9465
    • Tagore, R.1    Chen, H.2    Crabtree, R.H.3    Brudvig, G.W.4
  • 464
    • 0037507596 scopus 로고    scopus 로고
    • 18O isotope exchange measurements reveal that calcium is involved in the binding of one substrate-water molecule to the oxygen-evolving complex in photosystem II
    • DOI 10.1021/bi034279i
    • 18O isotope exchange measurements reveal that calcium is involved in the binding of one substrate-water molecule to the oxygenevolving complex in photosystem II. Biochemistry 42, 6209-6217 (2003) (Pubitemid 36605123)
    • (2003) Biochemistry , vol.42 , Issue.20 , pp. 6209-6217
    • Hendry, G.1    Wydrzynski, T.2
  • 465
    • 38949105199 scopus 로고    scopus 로고
    • Investigation of substrate water interactions at the highaffinity Mn site in the photosystem II oxygen-evolving complex
    • S. Singh, R. J. Debus, T. Wydrzynski and W. Hillier: Investigation of substrate water interactions at the highaffinity Mn site in the photosystem II oxygen-evolving complex. Phil Trans R Soc B 363, 1229-1235 (2008)
    • (2008) Phil Trans R Soc B , vol.363 , pp. 1229-1235
    • Singh, S.1    Debus, R.J.2    Wydrzynski, T.3    Hillier, W.4
  • 466
    • 0039597109 scopus 로고    scopus 로고
    • Structure of an active water molecule in the water-oxidizing complex of photosystem II as studied by FTIR spectroscopy
    • T. Noguchi and M. Sugiura: Structure of an active water molecule in the water-oxidizing complex of photosystem II as studied by FTIR spectroscopy. Biochemistry 39, 10943-10949 (2000)
    • (2000) Biochemistry , vol.39 , pp. 10943-10949
    • Noguchi, T.1    Sugiura, M.2
  • 467
    • 0038183812 scopus 로고    scopus 로고
    • 13C isotope labeling
    • DOI 10.1021/bi0341612
    • 13C isotope labeling. Biochemistry 42, 6035-6042 (2003) (Pubitemid 36605106)
    • (2003) Biochemistry , vol.42 , Issue.20 , pp. 6035-6042
    • Noguchi, T.1    Sugiura, M.2
  • 468
    • 0037207105 scopus 로고    scopus 로고
    • FTIR detection of water reactions during the flash-induced S-state cycle of the photosynthetic water-oxidizing complex
    • DOI 10.1021/bi020603i
    • T. Noguchi and M. Sugiura: FTIR detection of water reactions during the flash-induced S-state cycle of the photosynthetic water-oxidizing complex. Biochemistry 41, 15706-15712 (2002) (Pubitemid 36062475)
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15706-15712
    • Noguchi, T.1    Sugiura, M.2
  • 469
    • 0037133143 scopus 로고    scopus 로고
    • Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on S-state transitions
    • DOI 10.1021/bi011954k
    • T. Noguchi and M. Sugiura: Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on S-state transitions. Biochemistry 41, 2322-2330 (2002) (Pubitemid 34160894)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2322-2330
    • Noguchi, T.1    Sugiura, M.2
  • 470
    • 0037027302 scopus 로고    scopus 로고
    • 2 state of photosystem ii
    • DOI 10.1021/bi026246t
    • 2 state of photosystem II. Biochemistry 41, 13328-13334 (2002) (Pubitemid 35244723)
    • (2002) Biochemistry , vol.41 , Issue.44 , pp. 13328-13334
    • Hendry, G.1    Wydrzynski, T.2
  • 471
    • 0031150139 scopus 로고    scopus 로고
    • -1 range and quantitative infrared spectroscopy of aqueous solutions
    • -1 range and quantitative infrared spectroscopy of aqueous solutions. Anal Biochem 248, 234-245 (1997)
    • (1997) Anal Biochem , vol.248 , pp. 234-245
    • Venyaminov, S.Y.1    Prendergast, F.G.2
  • 472
    • 54349117457 scopus 로고    scopus 로고
    • Monitoring water reactions during the S-state cycle of the photosynthetic water-oxidizing center: Detection of the DOD bending vibrations by means of Fourier transform infrared spectroscopy
    • H. Suzuki, M. Sugiura and T. Noguchi: Monitoring water reactions during the S-state cycle of the photosynthetic water-oxidizing center: Detection of the DOD bending vibrations by means of Fourier transform infrared spectroscopy. Biochemistry 47, 11024-11030 (2008)
    • (2008) Biochemistry , vol.47 , pp. 11024-11030
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 473
    • 33746313252 scopus 로고    scopus 로고
    • The catalytic manganese cluster: Organization of the metal ions
    • Ed T. Wydrzynski and K. Satoh. Springer, Dordrecht
    • V. K. Yachandra: The Catalytic Manganese Cluster: Organization of the Metal Ions. In: Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase. Ed T. Wydrzynski and K. Satoh. Springer, Dordrecht, 235-260 (2005)
    • (2005) Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase , pp. 235-260
    • Yachandra, V.K.1
  • 474
    • 8144221721 scopus 로고    scopus 로고
    • xCa structures for the catalytic site and spectroscopic data
    • xCa structures for the catalytic site and spectroscopic data. Phys Chem Chem Phys 6, 4764-4771 (2004)
    • (2004) Phys Chem Chem Phys , vol.6 , pp. 4764-4771
    • Messinger, J.1
  • 475
    • 72949116337 scopus 로고    scopus 로고
    • 2 formation in photosystem II
    • 2 Formation in Photosystem II. Acc Chem Res 42, 1871-1880 (2009)
    • (2009) Acc Chem Res , vol.42 , pp. 1871-1880
    • Siegbahn, P.E.M.1
  • 476
    • 0002090963 scopus 로고
    • A molecular 'double-pivot' mechanism for water oxidation
    • J. B. Vincent and G. Christou: A Molecular 'Double-Pivot' Mechanism for Water Oxidation. Inorg Chim Acta 136, L41-L43 (1987)
    • (1987) Inorg Chim Acta , vol.136
    • Vincent, J.B.1    Christou, G.2
  • 480
    • 0035808638 scopus 로고    scopus 로고
    • Mechanism of photosynthetic water oxidation: Combining biophysical studies of photosystem II with inorganic model chemistry
    • J. S. Vrettos, J. Limburg and G. W. Brudvig: Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry. Biochim Biophys Acta 1503, 229-245 (2001)
    • (2001) Biochim Biophys Acta , vol.1503 , pp. 229-245
    • Vrettos, J.S.1    Limburg, J.2    Brudvig, G.W.3
  • 482
    • 0000575451 scopus 로고
    • Temperature-dependence of s-state transition in a thermophilic cyanobacterium, synechococcus vulcanus copeland measured by absorption changes in the ultraviolet region
    • H. Koike, B. Hanssum, Y. Inoue and G. Renger: Temperature-Dependence of S-State Transition in a Thermophilic Cyanobacterium, Synechococcus vulcanus Copeland Measured by Absorption Changes in the Ultraviolet Region. Biochim Biophys Acta 893, 524-533 (1987)
    • (1987) Biochim Biophys Acta , vol.893 , pp. 524-533
    • Koike, H.1    Hanssum, B.2    Inoue, Y.3    Renger, G.4
  • 483
    • 0026566266 scopus 로고
    • Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach
    • G. Renger and B. Hanssum: Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach. FEBS Lett 299, 28-32 (1992)
    • (1992) FEBS Lett , vol.299 , pp. 28-32
    • Renger, G.1    Hanssum, B.2
  • 485
    • 1942504766 scopus 로고    scopus 로고
    • Time-resolved oxygen production by PSII: Chasing chemical intermediates
    • DOI 10.1016/j.bbabio.2003.06.001, PII S0005272803001944
    • J. Clausen, R. J. Debus and W. Junge: Time-resolved oxygen production by PSII: chasing chemical intermediates. Biochim Biophys Acta 1655, 184-194 (2004) (Pubitemid 38526179)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 184-194
    • Clausen, J.1    Debus, R.J.2    Junge, W.3
  • 486
    • 0028344645 scopus 로고
    • Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex
    • F. Rappaport, M. Blanchard-Desce and J. Lavergne: Kinetics of Electron-Transfer and Electrochromic Change during the Redox Transitions of the Photosynthetic Oxygen-Evolving Complex. Biochim Biophys Acta 1184, 178-192 (1994) (Pubitemid 24080783)
    • (1994) Biochimica et Biophysica Acta - Bioenergetics , vol.1184 , Issue.2-3 , pp. 178-192
    • Rappaport, F.1    Blanchard-Desce, M.2    Lavergne, J.3
  • 487
    • 0342676543 scopus 로고
    • Studies on the nature of the water-oxidizing enzyme. 3. Spectral characterization of the intermediary redox states in the water-oxidizing enzyme system y
    • G. Renger and W. Weiss: Studies on the Nature of the Water-Oxidizing Enzyme. 3. Spectral Characterization of the Intermediary Redox States in the Water-Oxidizing Enzyme System Y. Biochim Biophys Acta 850, 184-196 (1986)
    • (1986) Biochim Biophys Acta , vol.850 , pp. 184-196
    • Renger, G.1    Weiss, W.2
  • 488
    • 33847453635 scopus 로고
    • Kinetics of manganese redox transitions in the oxygen-evolving apparatus of photosynthesis
    • J. P. Dekker, J. J. Plijter, L. Ouwehand and H. J. Van Gorkom: Kinetics of Manganese Redox Transitions in the Oxygen-Evolving Apparatus of Photosynthesis. Biochim Biophys Acta 767, 176-179 (1984)
    • (1984) Biochim Biophys Acta , vol.767 , pp. 176-179
    • Dekker, J.P.1    Plijter, J.J.2    Ouwehand, L.3    Van Gorkom, H.J.4
  • 490
    • 23444453385 scopus 로고    scopus 로고
    • Search for intermediates of photosynthetic water oxidation
    • DOI 10.1007/s11120-005-3480-1
    • J. Clausen and W. Junge: Search for intermediates of photosynthetic water oxidation. Photosynth Res 84, 339-345 (2005) (Pubitemid 41110667)
    • (2005) Photosynthesis Research , vol.84 , Issue.1-3 , pp. 339-345
    • Clausen, J.1    Junge, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.