메뉴 건너뛰기




Volumn 1837, Issue 10, 2014, Pages 1625-1634

Cationic screening of charged surface groups (carboxylates) affects electron transfer steps in photosystem-II water oxidation and quinone reduction

Author keywords

Chlorophyll fluorescence; Electrostatic screening; Manganese complex; Oxygen evolution; Photosynthesis; Water oxidation

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; CATION; CHLORIDE; CHLOROPHYLL; MONOVALENT CATION; QUINONE DERIVATIVE;

EID: 84905779343     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.07.012     Document Type: Article
Times cited : (14)

References (84)
  • 5
    • 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 2006 4455 4483 (Pubitemid 44816649)
    • (2006) Chemical Reviews , vol.106 , Issue.11 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 6
    • 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 2008 53 80 (Pubitemid 50289510)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 53-80
    • Renger, G.1    Renger, T.2
  • 7
    • 57749104826 scopus 로고    scopus 로고
    • Photosynthetic energy conversion: Natural and artificial
    • J. Barber Photosynthetic energy conversion: natural and artificial Chem. Soc. Rev. 38 2009 185 196
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 185-196
    • Barber, J.1
  • 8
    • 72949083473 scopus 로고    scopus 로고
    • Principles, efficiency, and blueprint character of solar-energy conversion in photosynthetic water oxidation
    • H. Dau, and I. Zaharieva Principles, efficiency, and blueprint character of solar-energy conversion in photosynthetic water oxidation Acc. Chem. Res. 42 2009 1861 1870
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1861-1870
    • Dau, H.1    Zaharieva, I.2
  • 9
    • 84859631223 scopus 로고    scopus 로고
    • Recent developments in research on water oxidation by photosystem II
    • H. Dau, I. Zaharieva, and M. Haumann Recent developments in research on water oxidation by photosystem II Curr. Opin. Chem. Biol. 16 2012 3 10
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 3-10
    • Dau, H.1    Zaharieva, I.2    Haumann, M.3
  • 10
    • 82755187256 scopus 로고    scopus 로고
    • Two tyrosines that changed the world: Interfacing the oxidizing power of photochemistry to water splitting in photosystem II
    • S. Styring, J. Sjöholm, and F. Mamedov Two tyrosines that changed the world: Interfacing the oxidizing power of photochemistry to water splitting in photosystem II Biochim. Biophys. Acta 1817 2012 76 87
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 76-87
    • Styring, S.1    Sjöholm, J.2    Mamedov, F.3
  • 11
    • 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
  • 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 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
  • 13
    • 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
  • 14
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.-R. Shen, and N. Kamiya Crystal structure of 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
  • 15
    • 33744992236 scopus 로고    scopus 로고
    • Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria (response letter)
    • H. Dau, and M. Haumann Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria (response letter) Science 312 2006 1471 1472
    • (2006) Science , vol.312 , pp. 1471-1472
    • Dau, H.1    Haumann, M.2
  • 16
    • 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 OO bond formation in oxygenic photosynthesis - a basic reaction cycle of the photosystem II manganese complex Biochim. Biophys. Acta 1767 2007 472 483 (Pubitemid 46860310)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 472-483
    • Dau, H.1    Haumann, M.2
  • 17
    • 84867049701 scopus 로고    scopus 로고
    • Alternating electron and proton transfer steps in photosynthetic water oxidation
    • A. Klauss, M. Haumann, and H. Dau Alternating electron and proton transfer steps in photosynthetic water oxidation Proc. Natl. Acad. Sci. U. S. A. 109 2012 16035 16040
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16035-16040
    • Klauss, A.1    Haumann, M.2    Dau, H.3
  • 18
    • 0015372336 scopus 로고
    • The ration between delayed light and fluorescence emitted by chloroplasts
    • W. Arnold The ration between delayed light and fluorescence emitted by chloroplasts Biophys. J. 12 1972 793 796
    • (1972) Biophys. J. , vol.12 , pp. 793-796
    • Arnold, W.1
  • 19
    • 0017281940 scopus 로고
    • Photoinduction kinetics of electrical potential in a single chloroplast as studied with micro-electrode technique
    • A.A. Bulychev, V.K. Andrianov, G.A. Kurella, and F.F. Litvin Photoinduction kinetics of electrical potential in a single chloroplast as studied with micro-electrode technique Biochim. Biophys. Acta 430 1976 336 351
    • (1976) Biochim. Biophys. Acta , vol.430 , pp. 336-351
    • Bulychev, A.A.1    Andrianov, V.K.2    Kurella, G.A.3    Litvin, F.F.4
  • 20
    • 0017229743 scopus 로고
    • The electrophotoluminescence of chloroplasts
    • J.L. Ellenson, and K. Sauer The electrophotoluminescence of chloroplasts Photochem. Photobiol. 23 1976 113 123
    • (1976) Photochem. Photobiol. , vol.23 , pp. 113-123
    • Ellenson, J.L.1    Sauer, K.2
  • 21
    • 0019317729 scopus 로고
    • The influence of the electric diffusion potential on delayed fluorescence light curves of chloroplasts treated with 3-(3,4-dichlorophenyl)-1,1- dimethylurea
    • P.S. Venediktov, V.N. Goltsev, and V.P. Shinkarev The influence of the electric diffusion potential on delayed fluorescence light curves of chloroplasts treated with 3-(3,4-dichlorophenyl)-1,1-dimethylurea Biochim. Biophys. Acta 593 1980 125 132
    • (1980) Biochim. Biophys. Acta , vol.593 , pp. 125-132
    • Venediktov, P.S.1    Goltsev, V.N.2    Shinkarev, V.P.3
  • 22
    • 4243622336 scopus 로고
    • Excitation trapping and charge separation in photosystem II in the presence of an electrical field
    • R.F. Meiburg, H.J. van Gorkom, and R.J. van Dorssen Excitation trapping and charge separation in photosystem II in the presence of an electrical field Biochim. Biophys. Acta 724 1983 352 358
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 352-358
    • Meiburg, R.F.1    Van Gorkom, H.J.2    Van Dorssen, R.J.3
  • 23
    • 0025728044 scopus 로고
    • Effect of light-induced changes in thylakoid voltage on chlorophyll fluorescence of Aegopodium podagraria leaves
    • H. Dau, R. Windecker, and U.P. Hansen Effect of light-induced changes in thylakoid voltage on chlorophyll fluorescence of Aegopodium podagraria leaves Biochim. Biophys. Acta 1057 1991 337 345
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 337-345
    • Dau, H.1    Windecker, R.2    Hansen, U.P.3
  • 24
    • 0026795667 scopus 로고
    • Electric field effect on the picosecond fluorescence of photosystem II and its relation to the energetics and kinetics of primary charge separation
    • H. Dau, and K. Sauer Electric field effect on the picosecond fluorescence of photosystem II and its relation to the energetics and kinetics of primary charge separation Biochim. Biophys. Acta 1102 1992 91 106
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 91-106
    • Dau, H.1    Sauer, K.2
  • 25
    • 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 2007 434 440 (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
  • 26
    • 84862168074 scopus 로고    scopus 로고
    • Extended protein/water H-bond networks in photosynthetic water oxidation
    • A.N. Bondar, and H. Dau Extended protein/water H-bond networks in photosynthetic water oxidation Biochim. Biophys. Acta 1817 2012 1177 1190
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1177-1190
    • Bondar, A.N.1    Dau, H.2
  • 27
    • 0015116719 scopus 로고
    • The role of cations in the organization of chloroplast membranes
    • S. Murakami, and L. Packer The role of cations in the organization of chloroplast membranes Arch. Biochem. Biophys. 146 1971 337 347
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 337-347
    • Murakami, S.1    Packer, L.2
  • 28
    • 0017889613 scopus 로고
    • Cation induced increase in chlorophyll fluorescence yield and the effect of electrical charge
    • DOI 10.1016/0014-5793(78)80708-X
    • J. Barber, and G.F.W. Searle Cation induced increase in chlorophyll fluorescence yield and effect of electrical charge FEBS Lett. 92 1978 5 8 (Pubitemid 8384818)
    • (1978) FEBS Letters , vol.92 , Issue.1 , pp. 5-8
    • Barber, J.1    Searle, G.F.W.2
  • 29
    • 0019273134 scopus 로고
    • Membrane surface charges and potentials in relation to photosynthesis
    • J. Barber Membrane surface charges and potentials in relation to photosynthesis Biochim. Biophys. Acta 594 1980 253 308
    • (1980) Biochim. Biophys. Acta , vol.594 , pp. 253-308
    • Barber, J.1
  • 30
    • 57849159013 scopus 로고    scopus 로고
    • Dynamic flexibility in the structure and function of photosystem II in higher plant thylakoid membranes: The grana enigma
    • DOI 10.1007/s11120-008-9381-3
    • J.M. Anderson, W.S. Chow, and J. De Las Rivas Dynamic flexibility in the structure and function of photosystem II in higher plant thylakoid membranes: the grana enigma Photosynth. Res. 98 2008 575 587 (Pubitemid 50326507)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 575-587
    • Anderson, J.M.1    Chow, W.S.2    De Las Rivas, J.3
  • 31
    • 0025052304 scopus 로고
    • Membrane electrostatics
    • G. Cevc Membrane electrostatics Biochim. Biophys. Acta 1031 1990 311 382
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 311-382
    • Cevc, G.1
  • 32
    • 20444495397 scopus 로고    scopus 로고
    • Energetics of primary and secondary electron transfer in Photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements
    • DOI 10.1016/j.bbabio.2005.03.007, PII S0005272805000897
    • M. Grabolle, and H. Dau Energetics of primary and secondary electron transfer in photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements Biochim. Biophys. Acta 1708 2005 209 218 (Pubitemid 40824951)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.2 , pp. 209-218
    • Grabolle, M.1    Dau, H.2
  • 33
    • 34249860034 scopus 로고    scopus 로고
    • Photosynthetic dioxygen formation studied by time-resolved delayed fluorescence measurements - Method, rationale, and results on the activation energy of dioxygen formation
    • DOI 10.1016/j.bbabio.2007.04.003, PII S0005272807000928, Structure and Function of Photosystems
    • J. Buchta, M. Grabolle, and H. Dau Photosynthetic dioxygen formation studied by time-resolved delayed fluorescence measurements - method, rationale, and results on the activation energy of dioxygen formation Biochim. Biophys. Acta 1767 2007 565 574 (Pubitemid 46860312)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 565-574
    • Buchta, J.1    Grabolle, M.2    Dau, H.3
  • 34
  • 37
    • 34547770303 scopus 로고    scopus 로고
    • Efficiency and role of loss processes in light-driven water oxidation by PSII
    • DOI 10.1111/j.1399-3054.2007.00941.x
    • M. Grabolle, and H. Dau Efficiency and role of loss processes in light-driven water oxidation by PSII Physiol. Plant. 131 2007 50 63 (Pubitemid 47228485)
    • (2007) Physiologia Plantarum , vol.131 , Issue.1 , pp. 50-63
    • Grabolle, M.1    Dau, H.2
  • 38
    • 0028155190 scopus 로고
    • Molecular mechanisms and quantitative models of variable Photosystem II fluorescence
    • H. Dau Molecular mechanisms and quantitative models of variable photosystem II fluorescence Photochem. Photobiol. 60 1994 1 23 (Pubitemid 2114483)
    • (1994) Photochemistry and Photobiology , vol.60 , Issue.1 , pp. 1-23
    • Dau, H.1
  • 39
    • 0014400748 scopus 로고
    • Analysis of the interactions between the two photosystems in isolated chloroplasts
    • P. Joliot, and A. Joliot Analysis of the interactions between the two photosystems in isolated chloroplasts Biochim. Biophys. Acta 153 1968 635 652
    • (1968) Biochim. Biophys. Acta , vol.153 , pp. 635-652
    • Joliot, P.1    Joliot, A.2
  • 41
    • 34547794990 scopus 로고    scopus 로고
    • Time-resolved X-ray spectroscopy leads to an extension of the classical S-state cycle model of photosynthetic oxygen evolution
    • DOI 10.1007/s11120-007-9141-9, Photosynthetic Water Oxidation
    • H. Dau, and M. Haumann Time-resolved X-ray spectroscopy leads to an extension of the classical S-state cycle model of photosynthetic oxygen evolution Photosynth. Res. 92 2007 327 343 (Pubitemid 47248571)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 327-343
    • Dau, H.1    Haumann, M.2
  • 43
    • 78649504612 scopus 로고    scopus 로고
    • 2O exchange and the influence of ph support formation of an intermediate by removal of a proton before dioxygen creation
    • 2O exchange and the influence of ph support formation of an intermediate by removal of a proton before dioxygen creation Biochemistry 49 2010 10098 10106
    • (2010) Biochemistry , vol.49 , pp. 10098-10106
    • Gerencser, L.1    Dau, H.2
  • 45
    • 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
  • 46
    • 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 transition 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
  • 47
    • 33645552565 scopus 로고    scopus 로고
    • Identification of a calcium-binding site in the PsbO protein of photosystem II
    • J.W. Murray, and J. Barber Identification of a calcium-binding site in the PsbO protein of photosystem II Biochemistry 45 2006 4128 4130
    • (2006) Biochemistry , vol.45 , pp. 4128-4130
    • Murray, J.W.1    Barber, J.2
  • 48
    • 84914593918 scopus 로고
    • Kinetic and energetic model for the primary processes in photosystem II
    • G.H. Schatz, H. Brock, and A.R. Holzwarth Kinetic and energetic model for the primary processes in photosystem II Biophys. J. 54 1988 397 405
    • (1988) Biophys. J. , vol.54 , pp. 397-405
    • Schatz, G.H.1    Brock, H.2    Holzwarth, A.R.3
  • 49
    • 0029006897 scopus 로고
    • Theory of fluorescence induction in photosystem II: Derivation of analytical expressions in a model including exciton-radical-pair equilibrium and restricted energy transfer between photosynthetic units
    • J. Lavergne, and H.W. Trissl Theory of fluorescence induction in photosystem II: derivation of analytical expressions in a model including exciton-radical-pair equilibrium and restricted energy transfer between photosynthetic units Biophys. J. 68 1995 2474 2492
    • (1995) Biophys. J. , vol.68 , pp. 2474-2492
    • Lavergne, J.1    Trissl, H.W.2
  • 50
    • 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
  • 51
    • 0019320156 scopus 로고
    • Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem II
    • J.M. Bowes, and A.R. Crofts Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem II Biochim. Biophys. Acta 590 1980 373 384
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 373-384
    • Bowes, J.M.1    Crofts, A.R.2
  • 52
    • 0342647009 scopus 로고    scopus 로고
    • Investigation of the plastoquinone pool size and fluorescence quenching in thylakoid membranes and Photosystem II (PS II) membrane fragments
    • DOI 10.1023/A:1006303510458
    • J. Kurreck, R. Schodel, and G. Renger Investigation of the plastoquinone pool size and fluorescence quenching in thylakoid membranes and photosystem II (PS II) membrane fragments Photosynth. Res. 63 2000 171 182 (Pubitemid 30427512)
    • (2000) Photosynthesis Research , vol.63 , Issue.2 , pp. 171-182
    • Kurreck, J.1    Schodel, R.2    Renger, G.3
  • 53
    • 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
  • 55
    • 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 1984 127 130
    • (1984) FEBS Lett. , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 56
    • 48549112394 scopus 로고
    • Structural and catalytic properties of the oxygen-evolving complex - Correlation of polypeptide and manganese release with the behavior of Z + in chloroplasts and a highly resolved preparation of the ps-ii complex
    • D.F. Ghanotakis, G.T. Babcock, and C.F. Yocum Structural and catalytic properties of the oxygen-evolving complex - correlation of polypeptide and manganese release with the behavior of Z + In chloroplasts and a highly resolved preparation of the ps-ii complex Biochim. Biophys. Acta 765 1984 388 398
    • (1984) Biochim. Biophys. Acta , vol.765 , pp. 388-398
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 57
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • R.J. Debus The manganese and calcium ions of photosynthetic oxygen evolution Biochim. Biophys. Acta 1102 1992 269 352
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 58
    • 0026792888 scopus 로고
    • 2 +-depleted photosystem II induced by binding of the 24-kilodalton extrinsic protein
    • 2 +-depleted photosystem II induced by binding of the 24-kilodalton extrinsic protein Biochemistry 31 1992 7648 7655
    • (1992) Biochemistry , vol.31 , pp. 7648-7655
    • Ono, T.A.1    Izawa, S.2    Inoue, Y.3
  • 60
    • 0028980975 scopus 로고
    • 2 + depletion modifies the electron-transfer on both donor and acceptor sides in photosystem II from spinach
    • 2 + depletion modifies the electron-transfer on both donor and acceptor sides in photosystem II from spinach Biochim. Biophys. Acta 1230 1995 155 164
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andreasson, L.E.1    Vass, I.2    Styring, S.3
  • 62
    • 0035861755 scopus 로고    scopus 로고
    • Substrate water exchange in photosystem II depends on the peripheral proteins
    • W. Hillier, G. Hendry, R.L. Burnap, and T. Wydrzynski Substrate water exchange in photosystem II depends on the peripheral proteins J. Biol. Chem. 276 2001 46917 46924
    • (2001) J. Biol. Chem. , vol.276 , pp. 46917-46924
    • Hillier, W.1    Hendry, G.2    Burnap, R.L.3    Wydrzynski, T.4
  • 63
    • 0037304618 scopus 로고    scopus 로고
    • 2 complex in response to a temperature jump: A time-resolved structural investigation employing x-ray absorption spectroscopy
    • 2 complex in response to a temperature jump: a time resolved structural investigation employing X-ray absorption spectroscopy Biophys. J. 84 2003 1370 1386 (Pubitemid 36133458)
    • (2003) Biophysical Journal , vol.84 , Issue.2 , pp. 1370-1386
    • Pospisl, P.1    Haumann, M.2    Dittmer, J.3    Sole, V.A.4    Dau, H.5
  • 64
    • 23444440334 scopus 로고    scopus 로고
    • Specific loss of the extrinsic 18 KDa protein from Photosystem II upon heating to 47°C causes inactivation of oxygen evolution likely due to Ca release from the Mn-complex
    • DOI 10.1007/s11120-004-7158-x
    • M. Barra, M. Haumann, and H. Dau Specific loss of the extrinsic 18 kDa protein from photosystem II upon heating to 47 °C causes inactivation of oxygen evolution likely due to Ca release from the Mn-complex Photosynth. Res. 84 2005 231 237 (Pubitemid 41110652)
    • (2005) Photosynthesis Research , vol.84 , Issue.1-3 , pp. 231-237
    • Barra, M.1    Haumann, M.2    Dau, H.3
  • 65
    • 33845307608 scopus 로고    scopus 로고
    • Intermediates in assembly by photoactivation after thermally accelerated disassembly of the manganese complex of photosynthetic water oxidation
    • DOI 10.1021/bi061842z
    • M. Barra, M. Haumann, P. Loja, R. Krivanek, A. Grundmeier, and H. Dau Intermediates in assembly by photoactivation after thermally accelerated disassembly of the manganese complex of photosynthetic water oxidation Biochemistry 45 2006 14523 14532 (Pubitemid 44868124)
    • (2006) Biochemistry , vol.45 , Issue.48 , pp. 14523-14532
    • Barra, M.1    Haumann, M.2    Loja, P.3    Krivanek, R.4    Grundmeier, A.5    Dau, H.6
  • 67
    • 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 2008 17384 17389
    • (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
  • 69
    • 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
  • 70
    • 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
  • 71
    • 33947139255 scopus 로고    scopus 로고
    • Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803
    • DOI 10.1016/j.bbabio.2007.01.022, PII S0005272807000254
    • K. Cser, and I. Vass Radiative and non-radiative charge recombination pathways in photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803 Biochim. Biophys. Acta 1767 2007 233 243 (Pubitemid 46400604)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.3 , pp. 233-243
    • Cser, K.1    Vass, I.2
  • 72
    • 63549106377 scopus 로고    scopus 로고
    • Janus-faced charge recombinations in photosystem II photoinhibition
    • I. Vass, and K. Cser Janus-faced charge recombinations in photosystem II photoinhibition Trends Plant Sci. 14 2009 200 205
    • (2009) Trends Plant Sci. , vol.14 , pp. 200-205
    • Vass, I.1    Cser, K.2
  • 73
    • 37549052159 scopus 로고    scopus 로고
    • Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1
    • P.B. Kos, Z. Deak, O. Cheregi, and I. Vass Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1 Biochim. Biophys. Acta 1777 2008 74 83
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 74-83
    • Kos, P.B.1    Deak, Z.2    Cheregi, O.3    Vass, I.4
  • 74
    • 38549155980 scopus 로고    scopus 로고
    • The psbA gene family responds differentially to light and UVB stress in Gloeobacter violaceus PCC 7421, a deeply divergent cyanobacterium
    • DOI 10.1016/j.bbabio.2007.09.001, PII S0005272807002046
    • C.I. Sicora, C.M. Brown, O. Cheregi, I. Vass, and D.A. Campbell The psbA gene family responds differentially to light and UVB stress in Gloeobacter violaceus PCC 7421, a deeply divergent cyanobacterium Biochim. Biophys. Acta 1777 2008 130 139 (Pubitemid 351162860)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.2 , pp. 130-139
    • Sicora, C.I.1    Brown, C.M.2    Cheregi, O.3    Vass, I.4    Campbell, D.A.5
  • 75
    • 57449108112 scopus 로고    scopus 로고
    • Low-oxygen induction of normally cryptic psbA genes in cyanobacteria
    • T.C. Summerfield, J. Toepel, and L.A. Sherman Low-oxygen induction of normally cryptic psbA genes in cyanobacteria Biochemistry 47 2008 12939 12941
    • (2008) Biochemistry , vol.47 , pp. 12939-12941
    • Summerfield, T.C.1    Toepel, J.2    Sherman, L.A.3
  • 76
    • 70749136825 scopus 로고    scopus 로고
    • Cyanobacterial psbA gene family: Optimization of oxygenic photosynthesis
    • P. Mulo, C. Sicora, and E.M. Aro Cyanobacterial psbA gene family: optimization of oxygenic photosynthesis Cell. Mol. Life Sci. 66 2009 3697 3710
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3697-3710
    • Mulo, P.1    Sicora, C.2    Aro, E.M.3
  • 77
    • 77956899459 scopus 로고    scopus 로고
    • Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection
    • J. Sander, M. Nowaczyk, J. Buchta, H. Dau, I. Vass, Z. Deák, M. Dorogi, M. Iwai, and M. Rögner Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection J. Biol. Chem. 285 2010 29851 29856
    • (2010) J. Biol. Chem. , vol.285 , pp. 29851-29856
    • Sander, J.1    Nowaczyk, M.2    Buchta, J.3    Dau, H.4    Vass, I.5    Deák, Z.6    Dorogi, M.7    Iwai, M.8    Rögner, M.9
  • 78
    • 77956908711 scopus 로고    scopus 로고
    • Differences in the interactions between the subunits of photosystem II dependent on D1 protein variants in the thermophilic cyanobacterium Thermosynechococcus elongatus
    • M. Sugiura, E. Iwai, H. Hayashi, and A. Boussac Differences in the interactions between the subunits of photosystem II dependent on D1 protein variants in the thermophilic cyanobacterium Thermosynechococcus elongatus J. Biol. Chem. 285 2010 30008 30018
    • (2010) J. Biol. Chem. , vol.285 , pp. 30008-30018
    • Sugiura, M.1    Iwai, E.2    Hayashi, H.3    Boussac, A.4
  • 79
    • 84867135315 scopus 로고    scopus 로고
    • Positive regulation of psbA gene expression by cis-encoded antisense RNAs in Synechocystis sp. PCC 6803
    • I. Sakurai, D. Stazic, M. Eisenhut, E. Vuorio, C. Steglich, W.R. Hess, and E.M. Aro Positive regulation of psbA gene expression by cis-encoded antisense RNAs in Synechocystis sp. PCC 6803 Plant Physiol. 160 2012 1000 1010
    • (2012) Plant Physiol. , vol.160 , pp. 1000-1010
    • Sakurai, I.1    Stazic, D.2    Eisenhut, M.3    Vuorio, E.4    Steglich, C.5    Hess, W.R.6    Aro, E.M.7
  • 80
    • 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 1991 10004 10012
    • (1991) Biochemistry , vol.30 , pp. 10004-10012
    • Rappaport, F.1    Lavergne, J.2
  • 81
    • 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 1993 279 296
    • (1993) Photosynth. Res. , vol.38 , pp. 279-296
    • Lavergne, J.1    Junge, W.2
  • 82
    • 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 1999 30387 30392
    • (1999) J. Biol. Chem. , vol.274 , pp. 30387-30392
    • Schlodder, E.1    Witt, H.T.2
  • 83
    • 0028047699 scopus 로고
    • Extent and rate of proton release by photosynthetic water oxidation in thylakoids: Electrostatic relaxation versus chemical production
    • M. Haumann, and W. Junge Extent and rate of proton release by photosynthetic water oxidation in thylakoids: electrostatic relaxation versus chemical production Biochemistry 33 1994 864 872 (Pubitemid 24058423)
    • (1994) Biochemistry , vol.33 , Issue.4 , pp. 864-872
    • Haumann, M.1    Junge, W.2
  • 84
    • 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. Boegershausen, A. Mulkidjanian, and W. Junge Function of tyrosine-Z in water oxidation by photosystem II: electrostatical promotor instead of hydrogen abstractor Biochemistry 37 1998 1131 1142 (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.