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Volumn 1817, Issue 1, 2012, Pages 26-43

Charge separation in Photosystem II: A comparative and evolutionary overview

Author keywords

Charge separation; Evolution; Photoprotection; Photosystem II; Quinone; Type II reaction center

Indexed keywords

BICARBONATE; CYTOCHROME B559; FORMIC ACID; IRON; NONHEME IRON PROTEIN; QUINONE DERIVATIVE;

EID: 82755181814     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.07.012     Document Type: Review
Times cited : (277)

References (193)
  • 1
    • 13244255068 scopus 로고
    • Model systems for photosynthesis. V. Electron transfer between chlorophyll and quinones in a lecithin matrix
    • G.S. Beddard, G. Porter, and G.M. Weese Model systems for photosynthesis. V. Electron transfer between chlorophyll and quinones in a lecithin matrix Proc R Soc London A 342 1975 317 325
    • (1975) Proc R Soc London A , vol.342 , pp. 317-325
    • Beddard, G.S.1    Porter, G.2    Weese, G.M.3
  • 3
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • DOI 10.1146/annurev.arplant.57.032905.105350
    • N. Nelson, and C.F. Yocum Structure and function of Photosystems I and II Annu Rev Plant Biol 57 2006 521 565 (Pubitemid 44061036)
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 4
    • 0029088458 scopus 로고
    • In vivo participation of a high-potential iron-sulfur protein as electron-donor to the photochemical reaction center of Rubrivivax gelatinosus
    • B. Schoepp, P. Parot, L. Menin, J. Gaillard, P. Richaud, and A. Vermeglio In vivo participation of a high-potential iron-sulfur protein as electron-donor to the photochemical reaction center of Rubrivivax gelatinosus Biochemistry 34 1995 11736 11742
    • (1995) Biochemistry , vol.34 , pp. 11736-11742
    • Schoepp, B.1    Parot, P.2    Menin, L.3    Gaillard, J.4    Richaud, P.5    Vermeglio, A.6
  • 5
    • 0028814333 scopus 로고
    • The high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans is competent in photosynthetic electron-transfer
    • A. Hochkoeppler, S. Ciurli, G. Venturoli, and D. Zannoni The high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans is competent in photosynthetic electron-transfer FEBS Lett 357 1995 70 74
    • (1995) FEBS Lett , vol.357 , pp. 70-74
    • Hochkoeppler, A.1    Ciurli, S.2    Venturoli, G.3    Zannoni, D.4
  • 7
    • 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 2008 273 295
    • (2008) Coord Chem Rev , vol.252 , pp. 273-295
    • Dau, H.1    Haumann, M.2
  • 8
    • 0034623416 scopus 로고    scopus 로고
    • Evolution - When did photosynthesis emerge on earth?
    • D.J. Des Marais Evolution - when did photosynthesis emerge on earth? Science 289 2000 1703 1705
    • (2000) Science , vol.289 , pp. 1703-1705
    • Des Marais, D.J.1
  • 10
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem II
    • H. Michel, and J. Deisenhofer Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem II Biochemistry 27 1988 1 7
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 11
    • 0024678988 scopus 로고
    • Photosystem II, the water-splitting enzyme
    • A.W. Rutherford Photosystem II, the water-splitting enzyme Trends Biochem Sci 14 1989 227 232
    • (1989) Trends Biochem Sci , vol.14 , pp. 227-232
    • Rutherford, A.W.1
  • 12
    • 57849160616 scopus 로고    scopus 로고
    • Comparison of bacterial reaction centers and photosystem II
    • DOI 10.1007/s11120-008-9369-z
    • L. Kalman, J.C. Williams, and J.P. Allen Comparison of bacterial reaction centers and Photosystem II Photosynth Res 98 2008 643 655 (Pubitemid 50300661)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 643-655
    • Kalman, L.1    Williams, J.C.2    Allen, J.P.3
  • 13
    • 0035368488 scopus 로고    scopus 로고
    • The heart of photosynthesis in glorious 3D
    • DOI 10.1016/S0968-0004(01)01874-6, PII S0968000401018746
    • A.W. Rutherford, and P. Faller The heart of photosynthesis in glorious 3D Trends Biochem Sci 26 2001 341 344 (Pubitemid 32530644)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.6 , pp. 341-344
    • Rutherford A.William1    Faller, P.2
  • 14
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria
    • R.E. Blankenship, M.T. Madigan, C.E. Bauer, Kluwer Academic Publishers Dordrecht
    • N.W. Woodbury, and J.P. Allen The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria R.E. Blankenship, M.T. Madigan, C.E. Bauer, Anoxygenic photosynthetic bacteria: advances in photosynthesis 1995 Kluwer Academic Publishers Dordrecht 527 557
    • (1995) Anoxygenic Photosynthetic Bacteria: Advances in Photosynthesis , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 15
    • 0002573184 scopus 로고
    • Visible absorption spectroscopy of chlorophylls
    • H. Scheer, CRC Press Inc. Boca Raton, FL
    • A.J. Hoff, and J. Amesz Visible absorption spectroscopy of chlorophylls H. Scheer, chlorophylls 1991 CRC Press Inc. Boca Raton, FL 723 738
    • (1991) Chlorophylls , pp. 723-738
    • Hoff, A.J.1    Amesz, J.2
  • 16
    • 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 2010 1141 1153
    • (2010) Chemphyschem , vol.11 , pp. 1141-1153
    • Renger, T.1    Schlodder, E.2
  • 17
    • 0016733275 scopus 로고
    • Picosecond kinetics of events leading to reaction center bacteriochlorophyll oxidation
    • K.J. Kaufmann, P.L. Dutton, T.L. Netzel, J.S. Leigh, and P.M. Rentzepis Picosecond kinetics of events leading to reaction center bacteriochlorophyll oxidation Science 188 1975 1301 1304
    • (1975) Science , vol.188 , pp. 1301-1304
    • Kaufmann, K.J.1    Dutton, P.L.2    Netzel, T.L.3    Leigh, J.S.4    Rentzepis, P.M.5
  • 18
    • 0001109508 scopus 로고
    • Picosecond detection of an intermediate in photochemical reaction of bacterial photosynthesis
    • M.G. Rockley, M.W. Windsor, R.J. Cogdell, and W.W. Parson picosecond detection of an intermediate in photochemical reaction of bacterial photosynthesis Proc Natl Acad Sci U S A 72 1975 2251 2255
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 2251-2255
    • Rockley, M.G.1    Windsor, M.W.2    Cogdell, R.J.3    Parson, W.W.4
  • 19
    • 0002079634 scopus 로고
    • Observation of a bacteriochlorophyll anion radical during the primary charge separation in a reaction center
    • W. Holzapfel, U. Finkele, W. Kaiser, D. Oesterhelt, H. Scheer, H.U. Stilz, and W. Zinth Observation of a bacteriochlorophyll anion radical during the primary charge separation in a reaction center Chem Phys Lett 160 1989 1 7
    • (1989) Chem Phys Lett , vol.160 , pp. 1-7
    • Holzapfel, W.1    Finkele, U.2    Kaiser, W.3    Oesterhelt, D.4    Scheer, H.5    Stilz, H.U.6    Zinth, W.7
  • 20
    • 0033034893 scopus 로고    scopus 로고
    • New and unexpected routes for ultrafast electron transfer in photosynthetic reaction centers
    • DOI 10.1016/S0014-5793(99)00810-8, PII S0014579399008108
    • M.E. van Brederode, and R. van Grondelle New and unexpected routes for ultrafast electron transfer in photosynthetic reaction centers FEBS Lett 455 1999 1 7 (Pubitemid 29322770)
    • (1999) FEBS Letters , vol.455 , Issue.1-2 , pp. 1-7
    • Van Brederode, M.E.1    Van Grondelle, R.2
  • 21
  • 22
    • 0025891869 scopus 로고
    • A chlorophyll tilted 30° relative to the membrane in the Photosystem II reaction center
    • F.J.E. van Mieghem, K. Satoh, and A.W. Rutherford A chlorophyll tilted 30° relative to the membrane in the Photosystem II reaction center Biochim Biophys Acta 1058 1991 379 385
    • (1991) Biochim Biophys Acta , vol.1058 , pp. 379-385
    • Van Mieghem, F.J.E.1    Satoh, K.2    Rutherford, A.W.3
  • 23
    • 0002799732 scopus 로고    scopus 로고
    • Photosystem II and the quinone-iron-containing reaction centers: Comparisons and evolutionary perspectives
    • H. Baltscheffsky, CVH New York
    • A.W. Rutherford, and W. Nitschke Photosystem II and the quinone-iron-containing reaction centers: comparisons and evolutionary perspectives H. Baltscheffsky, Origin and evolution of biological energy conversion 1996 CVH New York 143 175
    • (1996) Origin and Evolution of Biological Energy Conversion , pp. 143-175
    • Rutherford, A.W.1    Nitschke, W.2
  • 24
    • 0017127932 scopus 로고
    • Picosecond kinetics in reaction centers of Rps sphaeroides and effects of ubiquinone extraction and reconstitution
    • K.J. Kaufmann, K.M. Petty, P.L. Dutton, and P.M. Rentzepis Picosecond kinetics in reaction centers of Rps sphaeroides and effects of ubiquinone extraction and reconstitution Biochem Biophys Res Commun 70 1976 839 845
    • (1976) Biochem Biophys Res Commun , vol.70 , pp. 839-845
    • Kaufmann, K.J.1    Petty, K.M.2    Dutton, P.L.3    Rentzepis, P.M.4
  • 27
    • 0021674417 scopus 로고
    • Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • DOI 10.1021/bi00319a017
    • D. Kleinfeld, M.Y. Okamura, and G. Feher Electron transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state - evidence for light induced structural changes Biochemistry 23 1984 5780 5786 (Pubitemid 15189728)
    • (1984) Biochemistry , vol.23 , Issue.24 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 28
    • 0001228592 scopus 로고
    • Reaction center associated cytochromes
    • R.E. Blankenship, M.T. Madigan, C.E. Bauer, Kluwer Academic Publishers Dordrecht
    • W. Nitschke, and M. Dracheva Reaction center associated cytochromes R.E. Blankenship, M.T. Madigan, C.E. Bauer, Anoxygenic photosynthetic bacteria: advances in photosynthesis 1995 Kluwer Academic Publishers Dordrecht 527 557
    • (1995) Anoxygenic Photosynthetic Bacteria: Advances in Photosynthesis , pp. 527-557
    • Nitschke, W.1    Dracheva, M.2
  • 30
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides
    • d1-504
    • C.A. Wraight Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides Front Biosci 9 2004 309 337 (Pubitemid 38930849)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 31
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of Photosystem II of oxygenic photosynthesis
    • DOI 10.1146/annurev.arplant.53.100301.135238
    • B.A. Diner, and F. Rappaport Structure, dynamics, and energetics of the primary photochemistry of Photosystem II of oxygenic photosynthesis Ann Rev Plant Biol 53 2002 551 580 (Pubitemid 36257507)
    • (2002) Annual Review of Plant Biology , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 32
    • 0033679186 scopus 로고    scopus 로고
    • Primary charge separation in Photosystem II
    • J.P. Dekker, and R. van Grondelle Primary charge separation in Photosystem II Photosynth Res 63 2000 195 208
    • (2000) Photosynth Res , vol.63 , pp. 195-208
    • Dekker, J.P.1    Van Grondelle, R.2
  • 33
    • 38049011376 scopus 로고    scopus 로고
    • 4Ca cluster and to the evolution of molecular oxygen in Photosystem II
    • 4Ca cluster and to the evolution of molecular oxygen in Photosystem II Coord Chem Rev 252 2008 259 272
    • (2008) Coord Chem Rev , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 34
    • 0000087299 scopus 로고
    • Spectral properties of stabilized D1/D2/cytochrome b559 Photosystem II reaction center complex - Effects of Triton X-100, the redox state of pheophytin, and β-carotene
    • V.L. Teten'kin, B.A. Gulyaev, M. Seibert, and A.B. Rubin Spectral properties of stabilized D1/D2/cytochrome b559 Photosystem II reaction center complex - effects of Triton X-100, the redox state of pheophytin, and β-carotene FEBS Lett 250 1989 459 463
    • (1989) FEBS Lett , vol.250 , pp. 459-463
    • Teten'Kin, V.L.1    Gulyaev, B.A.2    Seibert, M.3    Rubin, A.B.4
  • 35
    • 0025183698 scopus 로고
    • D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligorrhiza: Correlation between complex integrity, spectroscopic properties, photochemical activity, and pigment composition
    • P. Braun, B.M. Greenberg, and A. Scherz D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligorrhiza - correlation between complex integrity, spectroscopic properties, photochemical activity, and pigment composition Biochemistry 29 1990 10376 10387 (Pubitemid 20384547)
    • (1990) Biochemistry , vol.29 , Issue.45 , pp. 10376-10387
    • Braun, P.1    Greenberg, B.M.2    Scherz, A.3
  • 38
    • 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 2008 105 119
    • (2008) Biophys J , vol.95 , pp. 105-119
    • Raszewski, G.1    Diner, B.A.2    Schlodder, E.3    Renger, T.4
  • 39
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of the oxygen-evolving Photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.R. Shen, and N. Kamiya Crystal structure of the oxygen-evolving Photosystem II at a resolution of 1.9 Å Nature 473 2011 55 60
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 40
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial Photosystem II at 2.9 Å resolution and the 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 and the role of quinones, lipids, channels and chloride Nat Struct Mol Biol 16 2009 334 342
    • (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
  • 41
    • 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.A. Madjet, F. Muh, 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 2009 12603 12614
    • (2009) J Phys Chem B , vol.113 , pp. 12603-12614
    • Madjet, M.E.A.1    Muh, F.2    Renger, T.3
  • 44
    • 33144472069 scopus 로고    scopus 로고
    • Kinetics and mechanism of electron transfer in intact Photosystem II and in the isolated reaction center: Pheophytin is the primary electron acceptor
    • A.R. Holzwarth, M.G. Muller, M. Reus, M. Nowaczyk, J. Sander, and M. Rogner Kinetics and mechanism of electron transfer in intact Photosystem II and in the isolated reaction center: pheophytin is the primary electron acceptor Proc Natl Acad Sci U S A 103 2006 6895 6900
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6895-6900
    • Holzwarth, A.R.1    Muller, M.G.2    Reus, M.3    Nowaczyk, M.4    Sander, J.5    Rogner, M.6
  • 45
    • 0035822664 scopus 로고    scopus 로고
    • Site-directed mutations at D1-His198 and D2-His197 of photosystem II in Synechocystis PCC 6803: Sites of primary charge separation and cation and triplet stabilization
    • DOI 10.1021/bi010121r
    • B.A. Diner, E. Schlodder, P.J. Nixon, W.J. Coleman, F. Rappaport, J. Lavergne, W.F.J. Vermaas, and D.A. Chisholm Site-directed mutations at D1-His198 and D2-His 97 of Photosystem II in Synechocystis PCC 6803: sites of primary charge separation and cation and triplet stabilization Biochemistry 40 2001 9265 9281 (Pubitemid 32730048)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9265-9281
    • Diner, B.A.1    Schlodder, E.2    Nixon, P.J.3    Coleman, W.J.4    Rappaport, F.5    Lavergne, J.6    Vermaas, W.F.J.7    Chisholm, D.A.8
  • 47
    • 33746576099 scopus 로고    scopus 로고
    • Charge separation in photosystem II core complexes induced by 690-730nm 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 2006 841 851 (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
  • 48
    • 21244494763 scopus 로고    scopus 로고
    • Theory of optical spectra of photosystem II reaction centers: Location of the triplet state and the identity of the primary electron donor
    • DOI 10.1529/biophysj.104.050294
    • G. Raszewski, W. Saenger, and T. Renger Theory of optical spectra of Photosystem II reaction centers: location of the triplet state and the identity of the primary electron donor Biophys J 88 2005 986 998 (Pubitemid 40983839)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 986-998
    • Raszewski, G.1    Saenger, W.2    Renger, T.3
  • 49
    • 38949084611 scopus 로고    scopus 로고
    • Site-directed mutations at D1-His198 and D1-Thr179 of photosystem II in Synechocystis sp. PCC 6803: Deciphering the spectral properties of the PSII reaction centre
    • DOI 10.1098/rstb.2007.2215, PII HRTQX8420285JQ1R
    • E. Schlodder, W.J. Coleman, P.J. Nixon, R.O. Cohen, T. Renger, and B.A. Diner Site-directed mutations at D1-His198 and D1-Thr179 of Photosystem II in Synechocystis sp PCC 6803: deciphering the spectral properties of the PSII reaction centre Philos Trans R Soc B 363 2008 1197 1202 (Pubitemid 351225985)
    • (2008) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.363 , Issue.1494 , pp. 1197-1202
    • Schlodder, E.1    Coleman, W.J.2    Nixon, P.J.3    Cohen, R.O.4    Renger, T.5    Diner, B.A.6
  • 50
    • 0018785120 scopus 로고
    • Orientation of the bacteriochlorophyll triplet and the primary ubiquinone acceptor of Rhodospirillum rubrum in membrane multilayers determined by ESR spectroscopy (I)
    • B.J. Hales, and A. Dasgupta Orientation of the bacteriochlorophyll triplet and the primary ubiquinone acceptor of Rhodospirillum rubrum in membrane multilayers determined by ESR spectroscopy (I) Biochim Biophys Acta 1979 548 1979 276 286
    • (1979) Biochim Biophys Acta , vol.1979 , Issue.548 , pp. 276-286
    • Hales, B.J.1    Dasgupta, A.2
  • 51
    • 0000231214 scopus 로고
    • Orientation of the primary quinone of bacterial photosynthetic reaction centers contained in chromatophore and reconstituted membranes/ion centers contained in chromatophore and reconstituted membranes
    • D.M. Tiede, and P.L. Dutton Orientation of the primary quinone of bacterial photosynthetic reaction centers contained in chromatophore and reconstituted membranes/ion centers contained in chromatophore and reconstituted membranes Biochim Biophys Acta 637 1981 278 290
    • (1981) Biochim Biophys Acta , vol.637 , pp. 278-290
    • Tiede, D.M.1    Dutton, P.L.2
  • 52
    • 0025163688 scopus 로고
    • Orientation of P700, the primary electron-donor of Photosystem i
    • A.W. Rutherford, and P. Setif Orientation of P700, the primary electron-donor of Photosystem I Biochim Biophys Acta 1019 1990 128 132
    • (1990) Biochim Biophys Acta , vol.1019 , pp. 128-132
    • Rutherford, A.W.1    Setif, P.2
  • 53
    • 0025366169 scopus 로고
    • Photosynthetic reaction center of green sulfur bacteria studied by EPR
    • DOI 10.1021/bi00468a005
    • W. Nitschke, U. Feiler, and A.W. Rutherford Photosynthetic reaction center of green sulfur bacteria studied by epr Biochemistry 29 1990 3834 3842 (Pubitemid 20151292)
    • (1990) Biochemistry , vol.29 , Issue.16 , pp. 3834-3842
    • Nitschke, W.1    Feiler, U.2    Rutherford, A.W.3
  • 55
    • 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 2001 739 743 (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
  • 57
    • 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 2004 1831 1838 (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
  • 58
    • 0028908351 scopus 로고
    • Charge recombination reactions in Photosystem II.1. yields, recombination pathways, and kinetics of the primary pair
    • F.J.E. 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 1995 4798 4813
    • (1995) Biochemistry , vol.34 , pp. 4798-4813
    • Van Mieghem, F.J.E.1    Brettel, K.2    Hillmann, B.3    Kamlowski, A.4    Rutherford, A.W.5    Schlodder, E.6
  • 59
    • 0028960993 scopus 로고
    • Charge recombination reactions in Photosystem II.2. Transient absorbency difference spectra and their temperature-dependence
    • B. Hillmann, K. Brettel, F.J.E. van Mieghem, A. Kamlowski, A.W. Rutherford, and E. Schlodder Charge recombination reactions in Photosystem II.2. Transient absorbency difference spectra and their temperature-dependence Biochemistry 34 1995 4814 4827
    • (1995) Biochemistry , vol.34 , pp. 4814-4827
    • Hillmann, B.1    Brettel, K.2    Van Mieghem, F.J.E.3    Kamlowski, A.4    Rutherford, A.W.5    Schlodder, E.6
  • 60
    • 0000029388 scopus 로고
    • The influence of the quinone-iron electron-acceptor complex on the reaction center photochemistry of Photosystem II
    • F.J.E. van Mieghem, W. Nitschke, P. Mathis, and A.W. Rutherford The influence of the quinone-iron electron-acceptor complex on the reaction center photochemistry of Photosystem II Biochim Biophys Acta 977 1989 207 214
    • (1989) Biochim Biophys Acta , vol.977 , pp. 207-214
    • Van Mieghem, F.J.E.1    Nitschke, W.2    Mathis, P.3    Rutherford, A.W.4
  • 64
    • 0032551757 scopus 로고    scopus 로고
    • Reaction centre photochemistry in cyanide-treated photosystem II
    • DOI 10.1016/S0005-2728(98)00091-7, PII S0005272898000917
    • Y. Deligiannakis, and A.W. Rutherford Reaction centre photochemistry in cyanide-treated Photosystem II Biochim Biophys Acta 1365 1998 354 362 (Pubitemid 29012393)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.3 , pp. 354-362
    • Deligiannakis, Y.1    Rutherford, A.W.2
  • 65
    • 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 2002 1112 1116 (Pubitemid 35337206)
    • (2002) Plant and Cell Physiology , vol.43 , Issue.10 , pp. 1112-1116
    • Noguchi, T.1
  • 71
    • 0002928340 scopus 로고
    • Electron transfer in Photosystem II
    • H.J. van Gorkom Electron transfer in Photosystem II Photosynth Res 6 1985 97 112
    • (1985) Photosynth Res , vol.6 , pp. 97-112
    • Van Gorkom, H.J.1
  • 73
    • 0037007996 scopus 로고    scopus 로고
    • Kinetics and pathways of charge recombination in photosystem II
    • DOI 10.1021/bi025725p
    • F. Rappaport, M. Guergova-Kuras, P.J. Nixon, B.A. Diner, and J. Lavergne Kinetics and pathways of charge recombination in Photosystem II Biochemistry 41 2002 8518 8527 (Pubitemid 34705507)
    • (2002) Biochemistry , vol.41 , Issue.26 , pp. 8518-8527
    • Rappaport, F.1    Guergova-Kuras, M.2    Nixon, P.J.3    Diner, B.A.4    Lavergne, J.5
  • 74
    • 70350434324 scopus 로고    scopus 로고
    • Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in Photosystem II
    • Y. Kato, M. Sugiura, A. Oda, and T. Watanabe Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in Photosystem II Proc Natl Acad Sci U S A 106 2009 17365 17370
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17365-17370
    • Kato, Y.1    Sugiura, M.2    Oda, A.3    Watanabe, T.4
  • 75
    • 77649324572 scopus 로고    scopus 로고
    • Redox potential of pheophytin a in Photosystem II of two cyanobacteria having the different special pair chlorophylls
    • S.I. Allakhverdiev, T. Tomo, Y. Shimada, H. Kindo, R. Nagao, V.V. Klimov, and M. Mimuro Redox potential of pheophytin a in Photosystem II of two cyanobacteria having the different special pair chlorophylls Proc Natl Acad Sci U S A 107 2010 3924 3929
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3924-3929
    • Allakhverdiev, S.I.1    Tomo, T.2    Shimada, Y.3    Kindo, H.4    Nagao, R.5    Klimov, V.V.6    Mimuro, M.7
  • 78
    • 0028344645 scopus 로고
    • Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex
    • F. Rappaport, M. Blancharddesce, and J. Lavergne Kinetics of electron-transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex Biochim Biophys Acta 1184 1994 178 192 (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
  • 79
    • 0031012149 scopus 로고    scopus 로고
    • Electron paramagnetic resonance kinetic studies of the S states in spinach thylakoids
    • DOI 10.1021/bi9614287
    • M.R. Razeghifard, C. Klughammer, and R.J. Pace Electron paramagnetic resonance kinetic studies of the S states in spinach thylakoids Biochemistry 36 1997 86 92 (Pubitemid 27024681)
    • (1997) Biochemistry , vol.36 , Issue.1 , pp. 86-92
    • Razeghifard, M.R.1    Klughammer, C.2    Pace, R.J.3
  • 80
    • 0035797872 scopus 로고    scopus 로고
    • B in photosystem II
    • DOI 10.1021/bi010852r
    • B in Photosystem II Biochemistry 40 2001 11912 11922 (Pubitemid 32906053)
    • (2001) Biochemistry , vol.40 , Issue.39 , pp. 11912-11922
    • De Wijn, R.1    Van Gorkom, H.J.2
  • 82
    • 0017845765 scopus 로고
    • Determination and modification of the redox state of the secondary acceptor of photosystem II in the dark
    • F.A. Wollman Determination and modification of redox state of secondary acceptor of Photosystem II in dark Biochim Biophys Acta 503 1978 263 273 (Pubitemid 8384366)
    • (1978) Biochimica et Biophysica Acta , vol.503 , Issue.2 , pp. 263-273
    • Wollman, F.A.1
  • 83
    • 0001488895 scopus 로고
    • Thermoluminescence as a probe of Photosystem II photochemistry - The origin of the flash-induced glow peaks
    • A.W. Rutherford, A.R. Crofts, and Y. Inoue Thermoluminescence as a probe of Photosystem II photochemistry - the origin of the flash-induced glow peaks Biochim Biophys Acta 682 1982 457 465
    • (1982) Biochim Biophys Acta , vol.682 , pp. 457-465
    • Rutherford, A.W.1    Crofts, A.R.2    Inoue, Y.3
  • 84
    • 49049126264 scopus 로고
    • Kinetics of the oxidation reduction reactions of the Photosystem II quinone acceptor complex, and the pathway for deactivation
    • H.H. Robinson, and A.R. Crofts Kinetics of the oxidation reduction reactions of the Photosystem II quinone acceptor complex, and the pathway for deactivation FEBS Lett 153 1983 221 226
    • (1983) FEBS Lett , vol.153 , pp. 221-226
    • Robinson, H.H.1    Crofts, A.R.2
  • 86
    • 0041844392 scopus 로고
    • Primary charge separation in bacterial photosynthesis - Oxidized chlorophylls and reduced pheophytin
    • J. Fajer, D.C. Brune, M. Davis, A. Forman, and L.D. Spaulding Primary charge separation in bacterial photosynthesis - oxidized chlorophylls and reduced pheophytin Proc Natl Acad Sci U S A 72 1975 4956 4960
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 4956-4960
    • Fajer, J.1    Brune, D.C.2    Davis, M.3    Forman, A.4    Spaulding, L.D.5
  • 87
    • 45749139149 scopus 로고    scopus 로고
    • Effect of charge distribution over a chlorophyll dimer on the redox potential of P680 in photosystem II as studied by density functional theory calculations
    • DOI 10.1021/bi8007998
    • R. Takahashi, K. Hasegawa, and T. Noguchi Effect of charge distribution over a chlorophyll dimer on the redox potential of P680 in Photosystein II as studied by density functional theory calculations Biochemistry 47 2008 6289 6291 (Pubitemid 351874219)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6289-6291
    • Takahashi, R.1    Hasegawa, K.2    Noguchi, T.3
  • 90
    • 77956824330 scopus 로고
    • Evolution of photosynthesis
    • J. Amesz, Elsevier Amsterdam
    • H.J. van Gorkom Evolution of photosynthesis J. Amesz, New Comprenhensive Biochemistry Vol. 15 1987 Elsevier Amsterdam 343 350
    • (1987) New Comprenhensive Biochemistry , vol.15 , pp. 343-350
    • Van Gorkom, H.J.1
  • 91
    • 0014623308 scopus 로고
    • Quantitative treatment of function of plastoquinone in photosynthesis
    • H.H. Stiehl, and H.T. Witt Quantitative treatment of function of plastoquinone in photosynthesis Z Naturforsch Pt B 24 1969 1588 1598
    • (1969) Z Naturforsch Pt B , vol.24 , pp. 1588-1598
    • Stiehl, H.H.1    Witt, H.T.2
  • 92
    • 0016158876 scopus 로고
    • Identification of reduced primary electron-acceptor of Photosystem II as a bound semiquinone anion
    • H.J. van Gorkom Identification of reduced primary electron-acceptor of Photosystem II as a bound semiquinone anion Biochim Biophys Acta 347 1974 439 442
    • (1974) Biochim Biophys Acta , vol.347 , pp. 439-442
    • Van Gorkom, H.J.1
  • 93
    • 0015417230 scopus 로고
    • Photochemical electron-transport in photosynthetic reaction centers.4. Observations related to reduced photoproducts
    • R.K. Clayton, and S.C. Straley Photochemical electron-transport in photosynthetic reaction centers.4. Observations related to reduced photoproducts Biophys J 12 1972 1221 1234
    • (1972) Biophys J , vol.12 , pp. 1221-1234
    • Clayton, R.K.1    Straley, S.C.2
  • 94
    • 0016291383 scopus 로고
    • Question of primary acceptor in bacterial photosynthesis - Manganese substituting for iron in reaction centers of Rhodopseudomonas spheroides R-26
    • G. Feher, R.A. Isaacson, J.D. McElroy, L.C. Ackerson, and M.Y. Okamura Question of primary acceptor in bacterial photosynthesis - manganese substituting for iron in reaction centers of Rhodopseudomonas spheroides R-26 Biochim Biophys Acta 368 1974 135 139
    • (1974) Biochim Biophys Acta , vol.368 , pp. 135-139
    • Feher, G.1    Isaacson, R.A.2    McElroy, J.D.3    Ackerson, L.C.4    Okamura, M.Y.5
  • 95
    • 0015911289 scopus 로고
    • Electron-transfer between 2 photosystems in spinach chloroplasts
    • B. Bouges-Bocquet Electron-transfer between 2 photosystems in spinach chloroplasts Biochim Biophys Acta 314 1973 250 256
    • (1973) Biochim Biophys Acta , vol.314 , pp. 250-256
    • Bouges-Bocquet, B.1
  • 96
    • 0015957318 scopus 로고
    • Charge accumulation at reducing side of System 2 of photosynthesis
    • B.R. Velthuys, and J. Amesz Charge accumulation at reducing side of System 2 of photosynthesis Biochim Biophys Acta 333 1974 85 94
    • (1974) Biochim Biophys Acta , vol.333 , pp. 85-94
    • Velthuys, B.R.1    Amesz, J.2
  • 97
    • 0017610719 scopus 로고
    • Electron acceptors of photosynthetic bacterial reaction centers. Direct observation of oscillatory behaviour suggesting two closely equivalent ubiquinones
    • C.A. Wraight Electron-acceptors of photosynthetic bacterial reaction centers - direct observation of oscillatory behavior suggesting 2 closely equivalent ubiquinones Biochim Biophys Acta 459 1977 525 531 (Pubitemid 8047539)
    • (1977) Biochimica et Biophysica Acta , vol.459 , Issue.3 , pp. 525-531
    • Wraight, C.A.1
  • 98
    • 0017392514 scopus 로고
    • Kinetics of electron transfer between the primary and the secondary electron acceptor in reaction centers from Rhodopseudomonas sphaeroides
    • A. Vermeglio, and R.K. Clayton Kinetics of electron transfer between primary and secondary electron acceptor in reaction centers from Rhodopseudomonas sphaeroides Biochim Biophys Acta 461 1977 159 165 (Pubitemid 8120610)
    • (1977) Biochimica et Biophysica Acta , vol.461 , Issue.1 , pp. 159-165
    • Vermeglio, A.1    Clayton, R.K.2
  • 99
    • 0017746823 scopus 로고
    • Reduction of pheophytin in the primary light reaction of photosystem II
    • DOI 10.1016/0014-5793(77)80580-2
    • V.V. Klimov, A.V. Klevanik, V.A. Shuvalov, and A.A. Krasnovsky Reduction of pheophytin in primary light reaction of Photosystem 2 FEBS Lett 82 1977 183 186 (Pubitemid 8206163)
    • (1977) FEBS Letters , vol.82 , Issue.2 , pp. 183-186
    • Klimov, V.V.1    Klevanik, A.V.2    Shuvalov, V.A.3    Krasnovsky, A.A.4
  • 100
    • 0019170329 scopus 로고
    • Interaction between the intermediary electron acceptor (pheophytin) and a possible plastoquinone-iron complex in photosystem II reaction centers
    • DOI 10.1073/pnas.77.12.7227
    • V.V. Klimov, E. Dolan, E.R. Shaw, and B. Ke Interaction between the intermediary electron-acceptor (pheophytin) and a possible plastoquinone-iron complex in Photosystem II reaction centers Proc Natl Acad Sci Biol 77 1980 7227 7231 (Pubitemid 11189446)
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , Issue.12 , pp. 7227-7231
    • Klimov, V.V.1    Dolan, E.2    Shaw, E.R.3    Ke, B.4
  • 101
    • 0017117596 scopus 로고
    • EPR properties of electron carrier intermediate between reaction center bacteriochlorophylls and primary acceptor in Chromatium vinosum
    • D.M. Tiede, R.C. Prince, G.H. Reed, and P.L. Dutton EPR properties of electron carrier intermediate between reaction center bacteriochlorophylls and primary acceptor in Chromatium vinosum FEBS Lett 65 1976 301 304
    • (1976) FEBS Lett , vol.65 , pp. 301-304
    • Tiede, D.M.1    Prince, R.C.2    Reed, G.H.3    Dutton, P.L.4
  • 102
    • 0019879108 scopus 로고
    • A light-induced spin-polarized triplet detected by electron paramagnetic res in Photosystem II reaction centers
    • A.W. Rutherford, D.R. Paterson, and J.E. Mullet A light-induced spin-polarized triplet detected by electron paramagnetic res in Photosystem II reaction centers Biochim Biophys Acta 635 1981 205 214
    • (1981) Biochim Biophys Acta , vol.635 , pp. 205-214
    • Rutherford, A.W.1    Paterson, D.R.2    Mullet, J.E.3
  • 103
    • 0015914840 scopus 로고
    • Primary events in photosynthetic reaction center from Rhodopseudomonas spheroides strain R26 - Triplet and oxidized states of bacteriochlorophyll and identification of primary electron-acceptor
    • P.L. Dutton, J.S. Leigh, and D.W. Reed Primary events in photosynthetic reaction center from Rhodopseudomonas spheroides strain R26 - Triplet and oxidized states of bacteriochlorophyll and identification of primary electron-acceptor Biochim Biophys Acta 292 1973 654 664
    • (1973) Biochim Biophys Acta , vol.292 , pp. 654-664
    • Dutton, P.L.1    Leigh, J.S.2    Reed, D.W.3
  • 104
    • 0016158698 scopus 로고
    • Reaction center bacteriochlorophyll triplet states - Redox potential dependence and kinetics
    • J.S. Leigh, and P.L. Dutton Reaction center bacteriochlorophyll triplet states - redox potential dependence and kinetics Biochim Biophys Acta 1974 357 1974 67 77
    • (1974) Biochim Biophys Acta , vol.1974 , Issue.357 , pp. 67-77
    • Leigh, J.S.1    Dutton, P.L.2
  • 105
    • 0016824530 scopus 로고
    • Triplet-state in bacterial photosynthesis - Possible mechanisms of primary photo-act
    • M.C. Thurnauer, J.J. Katz, and J.R. Norris Triplet-state in bacterial photosynthesis - possible mechanisms of primary photo-act Proc Natl Acad Sci U S A 72 1975 3270 3274
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 3270-3274
    • Thurnauer, M.C.1    Katz, J.J.2    Norris, J.R.3
  • 107
    • 0000983342 scopus 로고
    • Nanosecond fluorescence and absorbance changes in Photosystem II at low redox potential - Pheophytin as an intermediary electron acceptor
    • V.A. Shuvalov, V.V. Klimov, E. Dolan, W.W. Parson, and B. Ke Nanosecond fluorescence and absorbance changes in Photosystem II at low redox potential - pheophytin as an intermediary electron acceptor FEBS Lett 118 1980 279 282
    • (1980) FEBS Lett , vol.118 , pp. 279-282
    • Shuvalov, V.A.1    Klimov, V.V.2    Dolan, E.3    Parson, W.W.4    Ke, B.5
  • 108
    • 0000996241 scopus 로고
    • Direct detection of the electron-acceptor of Photosystem II - Evidence that Q is an iron-quinone complex
    • J.H.A. Nugent, B.A. Diner, and M.C.W. Evans Direct detection of the electron-acceptor of Photosystem II - evidence that Q is an iron-quinone complex FEBS Lett 124 1981 241 244
    • (1981) FEBS Lett , vol.124 , pp. 241-244
    • Nugent, J.H.A.1    Diner, B.A.2    Evans, M.C.W.3
  • 109
    • 0001304504 scopus 로고
    • A relationship between the midpoint potential of the primary acceptor and low-temperature photochemistry in Photosystem II
    • A.W. Rutherford, and P. Mathis A relationship between the midpoint potential of the primary acceptor and low-temperature photochemistry in Photosystem II FEBS Lett 154 1983 328 334
    • (1983) FEBS Lett , vol.154 , pp. 328-334
    • Rutherford, A.W.1    Mathis, P.2
  • 110
    • 0000865063 scopus 로고
    • Electron paramagnetic res measurements on the effects of bicarbonate and triazine resistance on the acceptor side of Photosystem II
    • W.F.J. Vermaas, and A.W. Rutherford Electron paramagnetic res measurements on the effects of bicarbonate and triazine resistance on the acceptor side of Photosystem II FEBS Lett 175 1984 243 248
    • (1984) FEBS Lett , vol.175 , pp. 243-248
    • Vermaas, W.F.J.1    Rutherford, A.W.2
  • 111
    • 48549108839 scopus 로고
    • A new electron paramagnetic res signal attributed to the primary plastosemiquinone acceptor in Photosystem II
    • A.W. Rutherford, and J.L. Zimmermann A new electron paramagnetic res signal attributed to the primary plastosemiquinone acceptor in Photosystem II Biochim Biophys Acta 767 1984 168 175
    • (1984) Biochim Biophys Acta , vol.767 , pp. 168-175
    • Rutherford, A.W.1    Zimmermann, J.L.2
  • 112
    • 0001967637 scopus 로고
    • How close is the analogy between the reaction centre of Photosystem II and that of purple bacteria? the electron acceptors side
    • J. Biggins, Nijhoff The Hague
    • A.W. Rutherford How close is the analogy between the reaction centre of Photosystem II and that of purple bacteria? The electron acceptors side J. Biggins, Progress in photosynthesis research 1987 Nijhoff The Hague 277 283
    • (1987) Progress in Photosynthesis Research , pp. 277-283
    • Rutherford, A.W.1
  • 113
    • 0029584591 scopus 로고
    • 13C-labeled bicarbonate
    • DOI 10.1021/bi00050a008
    • 13-labeled bicarbonate Biochemistry 34 1995 16288 16297 (Pubitemid 26006471)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16288-16297
    • Hienerwadel, R.1    Berthomieu, C.2
  • 114
    • 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 2009 2024 2033
    • (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
  • 115
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3A resolution
    • DOI 10.1038/318618a0
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution Nature 318 1985 618 624 (Pubitemid 16172409)
    • (1985) Nature , vol.318 , Issue.6047 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3
  • 116
    • 0000649240 scopus 로고
    • B binding polypeptide in the thylakoid membrane
    • B binding polypeptide in the thylakoid membrane Photosynth Res 10 1986 381 392
    • (1986) Photosynth Res , vol.10 , pp. 381-392
    • Trebst, A.1    Draber, W.2
  • 117
    • 84946632772 scopus 로고
    • Photosynthesis and the application of molecular genetics
    • Interceot Ltd., Newcaste-upon-Tyne
    • J. Barber, J.B. Marder, Photosynthesis and the application of molecular genetics, in: biotechnology and genetic engineering reviews 4, Interceot Ltd., Newcaste-upon-Tyne, 1986, pp. 355-404.
    • (1986) Biotechnology and Genetic Engineering Reviews 4 , pp. 355-404
    • Barber, J.1    Marder, J.B.2
  • 118
    • 0023029028 scopus 로고
    • The topology of a membrane protein: The orientation of the 32 kd Qb-binding chloroplast thylakoid membrane protein
    • B binding chloroplast thylakoid membrane protein Cell 47 1986 601 608 (Pubitemid 17215349)
    • (1986) Cell , vol.47 , Issue.4 , pp. 601-608
    • Sayre, R.T.1    Andersson, B.2    Bogorad, L.3
  • 119
    • 0001505435 scopus 로고
    • Isolation of a Photosystem II reaction center consisting of D1 and D2 polypeptides and cytochrome b559
    • O. Nanba, and K. Satoh Isolation of a Photosystem II reaction center consisting of D1 and D2 polypeptides and cytochrome b559 Proc Natl Acad Sci U S A 84 1987 109 112
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 109-112
    • Nanba, O.1    Satoh, K.2
  • 120
    • 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 1988 427 430
    • (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
  • 121
    • 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 O. 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 1988 8477 8481
    • (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
  • 122
    • 0025298292 scopus 로고
    • Structure of donor side components in Photosystem II predicted by computer modeling
    • B. Svensson, I. Vass, E. Cedergren, and S. Styring Structure of donor side components in Photosystem II predicted by computer modeling EMBO J 9 1990 2051 2059
    • (1990) EMBO J , vol.9 , pp. 2051-2059
    • Svensson, B.1    Vass, I.2    Cedergren, E.3    Styring, S.4
  • 123
    • 0034604258 scopus 로고    scopus 로고
    • - Radicals in photosystem II determined by high-field electron paramagnetic resonance
    • DOI 10.1021/bi000175l
    • • radicals in Photosystem II determined by high-field electron paramagnetic resonance Biochemistry 39 2000 7826 7834 (Pubitemid 30439612)
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7826-7834
    • Dorlet, P.1    Rutherford, A.W.2    Sun, U.3
  • 124
    • 67649452740 scopus 로고    scopus 로고
    • Configuration of electron transport components studied by EPR spectroscopy
    • T. Wydrzynski, S. Satoh, Springer Dordrecht
    • R. Bittl, and A. Kawamori Configuration of electron transport components studied by EPR spectroscopy T. Wydrzynski, S. Satoh, Photosystem II: the light-driven water:plastoquinone oxidoreductase 2005 Springer Dordrecht 389 402
    • (2005) Photosystem II: The Light-driven Water:plastoquinone Oxidoreductase , pp. 389-402
    • Bittl, R.1    Kawamori, A.2
  • 126
    • 0028913561 scopus 로고    scopus 로고
    • Spectroscopic evidence for the symmetrical location of tyrosine-D and tyrosine-Z in Photosystem II
    • D. Koulougliotis, X.S. Tang, B.A. Diner, and G.W. Brudvig Spectroscopic evidence for the symmetrical location of tyrosine-D and tyrosine-Z in Photosystem II Biochemistry 34 1999 2850 2856
    • (1999) Biochemistry , vol.34 , pp. 2850-2856
    • Koulougliotis, D.1    Tang, X.S.2    Diner, B.A.3    Brudvig, G.W.4
  • 128
    • 0030759919 scopus 로고    scopus 로고
    • Two-dimensional structure of plant photosystem II at 8-A resolution
    • DOI 10.1038/39103
    • K.H. Rhee, E.P. Morris, D. Zheleva, B. Hankamer, W. Kuhlbrandt, and J. Barber Two-dimensional structure of plant Photosystem II at 8 Å resolution Nature 389 1997 522 526 (Pubitemid 27435332)
    • (1997) Nature , vol.389 , Issue.6650 , pp. 522-526
    • Rhee, K.-H.1    Morris, E.P.2    Zheleva, D.3    Hankamer, B.4    Kuhlbrandt, W.5    Barber, J.6
  • 129
    • 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 2005 1040 1044 (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
  • 130
    • 0024997180 scopus 로고
    • Evolutionary relationships between 'Q-type' photosynthetic reaction centres: Hypothesis-testing using parsimony
    • DOI 10.1016/S0022-5193(05)80487-4
    • T.J. Beanland Evolutionary relationships between q-type photosynthetic reaction centers - hypothesis-testing using parsimony J Theor Biol 145 1990 535 545 (Pubitemid 20291475)
    • (1990) Journal of Theoretical Biology , vol.145 , Issue.4 , pp. 535-545
    • Beanland, T.J.1
  • 131
    • 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 1997 812 816 (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
  • 132
    • 52949129815 scopus 로고    scopus 로고
    • B site of the bacterial reaction center: A perspective from FTIR difference spectroscopy
    • B site of the bacterial reaction center: a perspective from FTIR difference spectroscopy Biochim Biophys Acta 1777 2008 1229 1248
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1229-1248
    • Nabedryk, E.1    Breton, J.2
  • 135
    • 78149409234 scopus 로고    scopus 로고
    • Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins
    • D. Onidas, J.M. Stachnik, S. Brucker, S. Kratzig, and K. Gerwert Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins Eur J Cell Biol 89 2010 983 989
    • (2010) Eur J Cell Biol , vol.89 , pp. 983-989
    • Onidas, D.1    Stachnik, J.M.2    Brucker, S.3    Kratzig, S.4    Gerwert, K.5
  • 136
    • 79953130211 scopus 로고    scopus 로고
    • Carboxylate shifts steer interquinone electron transfer in photosynthesis
    • P. Chernev, I. Zaharieva, H. Dau, and M. Haumann Carboxylate shifts steer interquinone electron transfer in photosynthesis J Biol Chem 286 2011 5368 5374
    • (2011) J Biol Chem , vol.286 , pp. 5368-5374
    • Chernev, P.1    Zaharieva, I.2    Dau, H.3    Haumann, M.4
  • 138
    • 0032577650 scopus 로고    scopus 로고
    • -.) formation in photosystem II
    • DOI 10.1016/S0014-5793(98)00491-8, PII S0014579398004918
    • -• formation in Photosystem II FEBS Lett 428 1998 123 126 (Pubitemid 28319670)
    • (1998) FEBS Letters , vol.428 , Issue.3 , pp. 123-126
    • Reifarth, F.1    Renger, G.2
  • 139
    • 0032544192 scopus 로고    scopus 로고
    • Correlation between protein flexibility and electron transfer from Q(A)/(-) to Q(B) in PSII membrane fragments from spinach
    • DOI 10.1021/bi980296+
    • B in PSII membrane fragments from spinach Biochemistry 37 1998 11399 11404 (Pubitemid 28388180)
    • (1998) Biochemistry , vol.37 , Issue.33 , pp. 11399-11404
    • Garbers, A.1    Reifarth, F.2    Kurreck, J.3    Renger, G.4    Parak, F.5
  • 140
    • 25444441462 scopus 로고    scopus 로고
    • Secondary quinone in photosystem II of Thermosynechococcus elongatus: Semiquinone-iron EPR signals and temperature dependence of electron transfer
    • DOI 10.1021/bi051000k
    • C. Fufezan, C.X. Zhang, A. Krieger-Liszkay, and A.W. Rutherford Secondary quinone in Photosystem II of Thermosynechococcus elongatus: semiquinone-iron EPR signals and temperature dependence of electron transfer Biochemistry 44 2005 12780 12789 (Pubitemid 41377317)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12780-12789
    • Fufezan, C.1    Zhang, C.2    Krieger-Liszkay, A.3    Rutherford, A.W.4
  • 143
    • 33746355593 scopus 로고    scopus 로고
    • Electrostatic role of the non-heme iron complex in bacterial photosynthetic reaction center
    • DOI 10.1016/j.febslet.2006.07.023, PII S0014579306008581
    • H. Ishikita, and E.-W. Knapp Electrostatic role of the non-heme iron complex in bacterial photosynthetic reaction center FEBS Lett 580 2006 4567 4570 (Pubitemid 44118272)
    • (2006) FEBS Letters , vol.580 , Issue.18 , pp. 4567-4570
    • Ishikita, H.1    Knapp, E.-W.2
  • 144
    • 79953802433 scopus 로고    scopus 로고
    • A site plastosemiquinone in the Photosystem II reaction centre
    • P.J. O'Malley
    • A site plastosemiquinone in the Photosystem II reaction centre P.J. O'Malley, J Phys Chem B 115 2011 4227 4233
    • (2011) J Phys Chem B , vol.115 , pp. 4227-4233
    • Lin, T.J.1
  • 147
    • 70449580488 scopus 로고    scopus 로고
    • A in Photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry
    • A in Photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry Biochemistry 48 2009 10682 10684
    • (2009) Biochemistry , vol.48 , pp. 10682-10684
    • Shibamoto, T.1    Kato, Y.2    Sugiura, M.3    Watanabe, T.4
  • 149
    • 55249086054 scopus 로고    scopus 로고
    • Multiple redox-active chlorophylls in the secondary electron transfer pathways of oxygen evolving Photosystem II
    • C.A. Tracewell, and G.W. Brudvig Multiple redox-active chlorophylls in the secondary electron transfer pathways of oxygen evolving Photosystem II Biochemistry 47 2008 11559 11572
    • (2008) Biochemistry , vol.47 , pp. 11559-11572
    • Tracewell, C.A.1    Brudvig, G.W.2
  • 151
    • 18744409047 scopus 로고    scopus 로고
    • Singlet oxygen production in herbicide-treated photosystem II
    • DOI 10.1016/S0014-5793(02)03724-9, PII S0014579302037249
    • C. Fufezan, A.W. Rutherford, and A. Krieger-Liszkay Singlet oxygen production in herbicide-treated Photosystem II FEBS Lett 532 2002 407 410 (Pubitemid 35441382)
    • (2002) FEBS Letters , vol.532 , Issue.3 , pp. 407-410
    • Fufezan, C.1    Rutherford, A.W.2    Krieger-Liszkay, A.3
  • 152
    • 0033005863 scopus 로고    scopus 로고
    • Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of
    • DOI 10.1016/S0005-2728(99)00005-5, PII S0005272899000055
    • N. Mizusawa, T. Yamashita, and M. Miyao Restoration of the high-potential form of cytochrome b559 of Photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions Biochim Biophys Acta 1410 1999 273 286 (Pubitemid 29114920)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1410 , Issue.3 , pp. 273-286
    • Mizusawa, N.1    Yamashita, T.2    Miyao, M.3
  • 153
    • 0029124281 scopus 로고
    • Granal Photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium
    • V.P. McNamara, and K. Gounaris Granal Photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium Biochim Biophys Acta 1231 1995 289 296
    • (1995) Biochim Biophys Acta , vol.1231 , pp. 289-296
    • McNamara, V.P.1    Gounaris, K.2
  • 154
    • 0022104260 scopus 로고
    • The effect of an applied elelctric field on the charge recombination kinetics in reaction centers reconstitutes in planar lipid bilayers
    • A. Gopher, Y. Blatty, D.M. Schonfeld, M.Y. Okamura, G. Feher, and M. Montal The effect of an applied elelctric field on the charge recombination kinetics in reaction centers reconstitutes in planar lipid bilayers Biophys J 48 1985 311 320
    • (1985) Biophys J , vol.48 , pp. 311-320
    • Gopher, A.1    Blatty, Y.2    Schonfeld, D.M.3    Okamura, M.Y.4    Feher, G.5    Montal, M.6
  • 155
    • 0023647477 scopus 로고
    • - state in reaction centers from Rhodopseudomonas viridis
    • - state in reaction centers from Rhodopseudomonas viridis Biochim Biophys Acta 893 1987 409 425
    • (1987) Biochim Biophys Acta , vol.893 , pp. 409-425
    • Shopes, R.J.1    Wraight, C.A.2
  • 156
    • 0023048040 scopus 로고
    • Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones or benzoquinones in place of ubiquinone
    • N.W. Woodbury, W.W. Parson, M.R. Gunner, R.C. Prince, and P.L. Dutton Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones or benzoquinones in place of ubiquinone Biochim Biophys Acta 851 1986 6 22
    • (1986) Biochim Biophys Acta , vol.851 , pp. 6-22
    • Woodbury, N.W.1    Parson, W.W.2    Gunner, M.R.3    Prince, R.C.4    Dutton, P.L.5
  • 157
    • 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 2005 14714 14720 (Pubitemid 41511009)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.42 , pp. 14714-14720
    • Ishikita, H.1    Knapp, E.-W.2
  • 158
    • 0032535220 scopus 로고    scopus 로고
    • Influence of herbicide binding on the redox potential of the quinone acceptor in photosystem II: Relevance to photodamage and phytotoxicity
    • DOI 10.1021/bi9822628
    • A. Krieger-Liszkay, and A.W. Rutherford Influence of herbicide binding on the redox potential of the quinone acceptor in Photosystem II. Relevance to photodamage and phytotoxicity Biochemistry 37 1998 17339 17344 (Pubitemid 29013734)
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17339-17344
    • Krieger-Liszkay, A.1    Rutherford, A.W.2
  • 159
    • 0028824726 scopus 로고
    • 4-clusters by preventing ligation of non-functional high-valency states of manganese
    • 4-clusters by preventing ligation of non-functional high-valency states of manganese Biochemistry 34 1995 13511 13526
    • (1995) Biochemistry , vol.34 , pp. 13511-13526
    • Chen, C.G.1    Kazimir, J.2    Cheniae, G.M.3
  • 160
    • 45949125703 scopus 로고
    • Photoactivation of the water-oxidizing complex in Photosystem II membranes depleted of mn and extrinsic proteins.1. Biochemical and kinetic characterization
    • N. Tamura, and G.M. Cheniae Photoactivation of the water-oxidizing complex in Photosystem II membranes depleted of mn and extrinsic proteins.1. Biochemical and kinetic characterization Biochim Biophys Acta 890 1987 179 194
    • (1987) Biochim Biophys Acta , vol.890 , pp. 179-194
    • Tamura, N.1    Cheniae, G.M.2
  • 161
  • 165
    • 11144285975 scopus 로고    scopus 로고
    • Purification, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus cultivated in a new type of photobioreactor
    • DOI 10.1016/j.bbabio.2004.10.007, PII S0005272804002956
    • J. Kern, B. Loll, C. Luneberg, D. DiFiore, J. Biesiadka, K.D. Irrgang, and A. Zouni Purification, characterisation and crystallisation of Photosystem II from Thermosynechococcus elongatus cultivated in a new type of photobioreactor Biochim Biophys Acta 1706 2005 147 157 (Pubitemid 40037770)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 147-157
    • Kern, J.1    Loll, B.2    Luneberg, C.3    DiFiore, D.4    Biesiadka, J.5    Irrgang, K.-D.6    Zouni, A.7
  • 166
    • 33846617289 scopus 로고    scopus 로고
    • Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559
    • DOI 10.1021/bi0613022
    • O. Kaminskaya, V.A. Shuvalov, and G. Renger Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559 Biochemistry 46 2007 1091 1105 (Pubitemid 46184996)
    • (2007) Biochemistry , vol.46 , Issue.4 , pp. 1091-1105
    • Kaminskaya, O.1    Shuvalov, V.A.2    Renger, G.3
  • 167
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids
    • J. Kruk, and K. Strzalka Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b559 in spinach thylakoids Photosynth Res 62 1999 273 279 (Pubitemid 30213282)
    • (1999) Photosynthesis Research , vol.62 , Issue.2-3 , pp. 273-279
    • Kruk, J.1    Strzalka, K.2
  • 168
    • 67649413283 scopus 로고    scopus 로고
    • Superoxide oxidase and reductase activity of cytochrome b559 in Photosystem II
    • A. Tiwari, and P. Pospisil Superoxide oxidase and reductase activity of cytochrome b559 in Photosystem II Biochim Biophys Acta 1787 2009 985 994
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 985-994
    • Tiwari, A.1    Pospisil, P.2
  • 171
    • 0026614703 scopus 로고
    • Photooxidation of cytochrome b559 in oxygen-evolving Photosystem II
    • C.A. Buser, B.A. Diner, and G.W. Brudvig Photooxidation of cytochrome b559 in oxygen-evolving Photosystem II Biochemistry 31 1992 11449 11459
    • (1992) Biochemistry , vol.31 , pp. 11449-11459
    • Buser, C.A.1    Diner, B.A.2    Brudvig, G.W.3
  • 172
    • 0024280216 scopus 로고
    • Cytochrome b559 may function to protect Photosystem II from photoinhibition
    • L.K. Thompson, and G.W. Brudvig Cytochrome b559 may function to protect Photosystem II from photoinhibition Biochemistry 27 1988 6653 6658
    • (1988) Biochemistry , vol.27 , pp. 6653-6658
    • Thompson, L.K.1    Brudvig, G.W.2
  • 174
  • 176
    • 0025781574 scopus 로고
    • β-carotene within the isolated Photosystem II reaction center - Photooxidation and irreversible bleaching of this chromophore by oxidized P680
    • A. Telfer, J.D. Rivas, and J. Barber β-carotene within the isolated Photosystem II reaction center - photooxidation and irreversible bleaching of this chromophore by oxidized P680 Biochim Biophys Acta 1060 1991 106 114
    • (1991) Biochim Biophys Acta , vol.1060 , pp. 106-114
    • Telfer, A.1    Rivas, J.D.2    Barber, J.3
  • 178
    • 79953178611 scopus 로고    scopus 로고
    • A high redox potential form of Cytochrome c550 in Photosystem II from Thermosynechococcus elongatus
    • F. Guerrero, A. Sedoud, D. Kirilovsky, A.W. Rutherford, J.M. Ortega, and M. Roncel A high redox potential form of Cytochrome c550 in Photosystem II from Thermosynechococcus elongatus J Biol Chem 286 2011 5985 5994
    • (2011) J Biol Chem , vol.286 , pp. 5985-5994
    • Guerrero, F.1    Sedoud, A.2    Kirilovsky, D.3    Rutherford, A.W.4    Ortega, J.M.5    Roncel, M.6
  • 179
    • 36849063196 scopus 로고    scopus 로고
    • The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution
    • J.W. Murray, K. Maghlaoui, and J. Barber The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 Å resolution Acta Crystallogr F 63 2007
    • (2007) Acta Crystallogr F , vol.63
    • Murray, J.W.1    Maghlaoui, K.2    Barber, J.3
  • 180
    • 0001700716 scopus 로고
    • 400, a high potential electron acceptor of Photosystem II, with the iron of the quinone-iron acceptor complex
    • 400, a high potential electron acceptor of Photosystem II, with the iron of the quinone-iron acceptor complex Biochim Biophys Acta 849 1986 264 275
    • (1986) Biochim Biophys Acta , vol.849 , pp. 264-275
    • Petrouleas, V.1    Diner, B.A.2
  • 181
    • 0028606120 scopus 로고
    • Binding of carboxylate anions at the nonheme FeII of PS-II.2. Competition with bicarbonate and effects on the QA/QB electron-transfer rate
    • V. Petrouleas, Y. Deligiannakis, and B.A. Diner Binding of carboxylate anions at the nonheme FeII of PS-II.2. Competition with bicarbonate and effects on the QA/QB electron-transfer rate Biochim Biophys Acta 1188 1994 271 277
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 271-277
    • Petrouleas, V.1    Deligiannakis, Y.2    Diner, B.A.3
  • 183
    • 0035795165 scopus 로고    scopus 로고
    • Photoreducible high spin iron electron paramagnetic resonance signals in dark-adapted Photosystem II: Are they oxidised non-haem iron formed from interaction of oxygen with PSII electron acceptors?
    • DOI 10.1016/S0005-2728(00)00257-7, PII S0005272800002577
    • J.H.A. Nugent Photoreducible high spin iron electron paramagnetic resonance signals in dark-adapted Photosystem II: are they oxidised non-haem iron formed from interaction of oxygen with PSII electron acceptors? Biochim Biophys Acta 1504 2001 288 298 (Pubitemid 32201900)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1504 , Issue.2-3 , pp. 288-298
    • Nugent, J.H.A.1
  • 184
    • 78249233837 scopus 로고    scopus 로고
    • Probing the quinone binding site of Photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides
    • A. Boussac, M. Sugiura, and F. Rappaport Probing the quinone binding site of Photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides Biochim Biophys Acta 1807 2011 119 129
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 119-129
    • Boussac, A.1    Sugiura, M.2    Rappaport, F.3
  • 186
    • 0010999318 scopus 로고
    • The iron-quinone acceptor complex in Rhodospirillum rubrum chromatophores studied by electron paramagnetic resonance
    • C. Beijer, and A.W. Rutherford The iron-quinone acceptor complex in Rhodospirillum rubrum chromatophores studied by electron paramagnetic resonance Biochim Biophys Acta 890 1987 169 178
    • (1987) Biochim Biophys Acta , vol.890 , pp. 169-178
    • Beijer, C.1    Rutherford, A.W.2
  • 187
    • 0024972738 scopus 로고
    • Absence of a bicarbonate-depletion effect in electron-transfer between quinones in chromatophores and reaction centers of Rhodobacter sphaeroides
    • R.J. Shopes, D.J. Blubaugh, C.A. Wraight, and Govindjee Absence of a bicarbonate-depletion effect in electron-transfer between quinones in chromatophores and reaction centers of Rhodobacter sphaeroides Biochim Biophys Acta 974 1989 114 118
    • (1989) Biochim Biophys Acta , vol.974 , pp. 114-118
    • Shopes, R.J.1    Blubaugh, D.J.2    Wraight, C.A.3    Govindjee4
  • 188
    • 0017062641 scopus 로고
    • Major site of bicarbonate effect in system-II reaction evidence from ESR signal-IIvf, fast fluorescence yield changes and delayed light-emission
    • P. Jursinic, J. Warden, and Govindjee Major site of bicarbonate effect in system-II reaction evidence from ESR signal-IIvf, fast fluorescence yield changes and delayed light-emission Biochim Biophys Acta 440 1976 322 330
    • (1976) Biochim Biophys Acta , vol.440 , pp. 322-330
    • Jursinic, P.1    Warden, J.2    Govindjee3
  • 189
    • 0017691989 scopus 로고
    • Investigation of the absorption changes of the plastoquinone system in broken chloroplasts. The effect of bicarbonate-depletion
    • U. Siggel, R. Khanna, G. Renger, and Govindjee Investigation of absorption changes of plastoquinone system in broken chloroplasts - Effect of bicarbonate depletion Biochim Biophys Acta 462 1977 196 207 (Pubitemid 8232620)
    • (1977) Biochimica et Biophysica Acta , vol.462 , Issue.1 , pp. 196-207
    • Siggel, U.1    Khanna, R.2    Renger, G.3    Govindjee4
  • 190
    • 84944003893 scopus 로고
    • The effects of bicarbonate depletion and formate incubation on the kinetics of oxidation-reduction reactions of the Photosystem II quinone acceptor complex
    • H.H. Robinson, J.J. Eaton-Rye, J.J.S. van Rensen, and Govindjee The effects of bicarbonate depletion and formate incubation on the kinetics of oxidation-reduction reactions of the Photosystem II quinone acceptor complex Z Naturforsch C 39 1984 382 385
    • (1984) Z Naturforsch C , vol.39 , pp. 382-385
    • Robinson, H.H.1    Eaton-Rye, J.J.2    Van Rensen, J.J.S.3    Govindjee4
  • 193
    • 0037085023 scopus 로고    scopus 로고
    • The rate of charge recombination in Photosystem II
    • DOI 10.1016/S0005-2728(02)00183-4, PII S0005272802001834
    • R. De Wijn, and H.J. van Gorkom The rate of charge recombination in Photosystem II Biochim. Biophys. Acta 1553 2002 302 308 (Pubitemid 34454768)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1553 , Issue.3 , pp. 302-308
    • De Wijn, R.1    Van Gorkom, H.J.2


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