메뉴 건너뛰기




Volumn 100, Issue 4, 1997, Pages 828-841

Mechanistic and structural aspects of photosynthetic water oxidation

Author keywords

Kinetic isotope effects; Oxygen evolution; Photosysterl II; Reaction coor dinates; Structure function relationships

Indexed keywords


EID: 0030773197     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1000409.x     Document Type: Article
Times cited : (83)

References (93)
  • 3
    • 0000659527 scopus 로고
    • A mass spectroscopic analysis of the water-splitting reaction
    • Bader, K. P., Renger, G. & Schmid, G. H. 1993. A mass spectroscopic analysis of the water-splitting reaction. - Photosynth. Res. 38: 355-361.
    • (1993) Photosynth. Res. , vol.38 , pp. 355-361
    • Bader, K.P.1    Renger, G.2    Schmid, G.H.3
  • 4
    • 0000684952 scopus 로고
    • The oxygen evolving complex in photosystem II as a metallo-radical enzyme
    • P. Mathis, ed., Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3858-8
    • Babcock, G. T. 1995. The oxygen evolving complex in photosystem II as a metallo-radical enzyme. - In Photosynthesis: From Light to Biosphere, Vol. II (P. Mathis, ed.), pp. 209-215. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3858-8.
    • (1995) Photosynthesis: from Light to Biosphere , vol.2 , pp. 209-215
    • Babcock, G.T.1
  • 7
    • 0025008019 scopus 로고
    • Histidine oxidation in the oxygen-evolving photosystem II enzyme
    • Boussac, A., Zimmermann, J. L., Rutherford, A. W. & Lavergne, J. 1990. Histidine oxidation in the oxygen-evolving photosystem II enzyme. - Nature 347: 303-306.
    • (1990) Nature , vol.347 , pp. 303-306
    • Boussac, A.1    Zimmermann, J.L.2    Rutherford, A.W.3    Lavergne, J.4
  • 8
    • 0029941460 scopus 로고    scopus 로고
    • Conversion of the spin state of the manganese complex in photosystem II induced by near-infrared light
    • _, Girerd, J.-J. & Rutherford, A. W. 1996. Conversion of the spin state of the manganese complex in photosystem II induced by near-infrared light. - Biochemistry 35: 6984-6989.
    • (1996) Biochemistry , vol.35 , pp. 6984-6989
    • Girerd, J.-J.1    Rutherford, A.W.2
  • 10
    • 0000561603 scopus 로고    scopus 로고
    • Oxygen evolution
    • D. R. Ort and C. F. Yocum, eds. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3683-6
    • Britt, R. D. 1996. Oxygen evolution. - In Oxygenic Photosynthesis: The Light Reactions (D. R. Ort and C. F. Yocum, eds), pp. 137-164. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3683-6.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 137-164
    • Britt, R.D.1
  • 11
    • 0004736638 scopus 로고
    • EPR spectroscopy of manganese enzymes
    • A. J. Hoff, ed., Elsevier, Amsterdam. ISBN 0-444-88050-X
    • Brudvig, G. W. 1989. EPR spectroscopy of manganese enzymes. - In Advanced EPR: Applications in Biology and Chemistry (A. J. Hoff, ed.), pp. 839-863. Elsevier, Amsterdam. ISBN 0-444-88050-X.
    • (1989) Advanced EPR: Applications in Biology and Chemistry , pp. 839-863
    • Brudvig, G.W.1
  • 12
    • 0029670613 scopus 로고    scopus 로고
    • 2O oxidation complex in Synechocystis sp. PCC6803
    • 2O oxidation complex in Synechocystis sp. PCC6803. - Biochemistry 35: 874-882.
    • (1996) Biochemistry , vol.35 , pp. 874-882
    • Burnap, R.L.1    Qian, M.2    Pierce, P.3
  • 13
    • 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: 13511-13526.
    • (1995) Biochemistry , vol.34 , pp. 13511-13526
    • Chen, C.1    Kazimir, J.2    Cheniae, G.M.3
  • 14
    • 8544246786 scopus 로고    scopus 로고
    • Investigations on the role of protonation steps in electron transfer reactions in Tris-treated PS II membrane fragments
    • Christen, G., Karge, M., Eckert, H.-J. & Renger, G. 1997. Investigations on the role of protonation steps in electron transfer reactions in Tris-treated PS II membrane fragments. - Photosynthetica 33: 529-539.
    • (1997) Photosynthetica , vol.33 , pp. 529-539
    • Christen, G.1    Karge, M.2    Eckert, H.-J.3    Renger, G.4
  • 15
    • 0029033834 scopus 로고
    • Amino acid residues that influence the binding of manganese or calcium to photosystem II. 1. The luminal interhelical domains of the D1 polypeptide
    • Chu, H. A., Nguyen, A. P. & Debus, R. J. 1995a. Amino acid residues that influence the binding of manganese or calcium to photosystem II. 1. The luminal interhelical domains of the D1 polypeptide. - Biochemistry 34: 5839-5858.
    • (1995) Biochemistry , vol.34 , pp. 5839-5858
    • Chu, H.A.1    Nguyen, A.P.2    Debus, R.J.3
  • 16
    • 0029071492 scopus 로고
    • Amino acid residues that influence the binding of manganese or calcium to photosystem II. 2. The carboxyl-terminal domain of the D1 polypeptide
    • _, Nguyen, A. P. & Debus, R. J. 1995b. Amino acid residues that influence the binding of manganese or calcium to photosystem II. 2. The carboxyl-terminal domain of the D1 polypeptide. - Biochemistry 34: 5859-5882.
    • (1995) Biochemistry , vol.34 , pp. 5859-5882
    • Nguyen, A.P.1    Debus, R.J.2
  • 17
    • 0000222974 scopus 로고
    • A model for the mechanism of chloride activation of oxygen evolution in photosystem II
    • Coleman, W. J. & Govindjee. 1987. A model for the mechanism of chloride activation of oxygen evolution in photosystem II. - Photosynth. Res. 13: 199-223.
    • (1987) Photosynth. Res. , vol.13 , pp. 199-223
    • Coleman, W.J.1    Govindjee2
  • 18
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts, A. R. & Wraight, C. A. 1983. The electrochemical domain of photosynthesis. - Biochim. Biophys. Acta 726: 149-185.
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 19
    • 0029806796 scopus 로고    scopus 로고
    • Unraveling the kinetic complexity of interprotein electron transfer reactions
    • Davidson, V. L. 1996. Unraveling the kinetic complexity of interprotein electron transfer reactions. - Biochemistry 35: 14035-14039.
    • (1996) Biochemistry , vol.35 , pp. 14035-14039
    • Davidson, V.L.1
  • 21
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis
    • Deisenhofer, J., Epp, O., Sinning, I. & Michel, H. 1995. Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. - J. Mol. Biol. 246: 429-457.
    • (1995) J. Mol. Biol. , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Sinning, I.3    Michel, H.4
  • 22
    • 0028448809 scopus 로고
    • Comparison of the manganese oxygen-evolving complex in photosystem II of spinach and Synechocystis sp. with multinuclear manganese model compounds by X-ray absorption spectroscopy
    • DeRose, V. J., Mukerji, I., Latimer, M. J., Yachandra, V. K., Sauer, K. & Klein, M. P. 1994. Comparison of the manganese oxygen-evolving complex in photosystem II of spinach and Synechocystis sp. with multinuclear manganese model compounds by X-ray absorption spectroscopy. - J. Am. Chem. Soc. 116: 5239-5249.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5239-5249
    • Derose, V.J.1    Mukerji, I.2    Latimer, M.J.3    Yachandra, V.K.4    Sauer, K.5    Klein, M.P.6
  • 23
    • 0001090546 scopus 로고
    • Intermediates of a polynuclear manganese center involved in photosynthetic oxidation of water
    • Dismukes, G. C. & Siderer, Y. 1981. Intermediates of a polynuclear manganese center involved in photosynthetic oxidation of water. - Proc. Natl. Acad. Sci. USA 78: 274-278.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 274-278
    • Dismukes, G.C.1    Siderer, Y.2
  • 24
  • 25
    • 0028829367 scopus 로고
    • Isolation and characterization of a photosystem II complex from the red alga Cyanidium caldarium: Association of cytochrome c-550 and a 12 kDa protein with the complex
    • Enami, I., Murayama, H., Ohta, H., Kamo, M., Nakazato, K. & Shen, J.-R. 1995. Isolation and characterization of a photosystem II complex from the red alga Cyanidium caldarium: Association of cytochrome c-550 and a 12 kDa protein with the complex. - Biochim. Biophys. Acta 1232: 208-216.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 208-216
    • Enami, I.1    Murayama, H.2    Ohta, H.3    Kamo, M.4    Nakazato, K.5    Shen, J.-R.6
  • 26
    • 0028188535 scopus 로고
    • Inactivation of the water oxidizing enzyme in MSP free mutant cells of the cyanobacteria Synechococcus PCC 7942 and Synechocystis PCC 6803 during dark incubation and conditions leading to photoactivation
    • Engels, D. H., Lott, A., Schmid, G. H. & Pistorius, E. K. 1994. Inactivation of the water oxidizing enzyme in MSP free mutant cells of the cyanobacteria Synechococcus PCC 7942 and Synechocystis PCC 6803 during dark incubation and conditions leading to photoactivation. - Photosynth. Res. 42: 227-244.
    • (1994) Photosynth. Res. , vol.42 , pp. 227-244
    • Engels, D.H.1    Lott, A.2    Schmid, G.H.3    Pistorius, E.K.4
  • 27
    • 0029914076 scopus 로고    scopus 로고
    • EPR and ENDOR studies on the water oxidizing complex of photosystem II
    • Fiege, R., Zweygart, W., Bittl, R., Adir, N., Renger, G. & Lubitz, W. 1996. EPR and ENDOR studies on the water oxidizing complex of photosystem II. - Photosynth. Res. 48: 227-237.
    • (1996) Photosynth. Res. , vol.48 , pp. 227-237
    • Fiege, R.1    Zweygart, W.2    Bittl, R.3    Adir, N.4    Renger, G.5    Lubitz, W.6
  • 29
    • 0028032823 scopus 로고
    • Functional characterization of mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll-protein CP47 in photosystem II
    • Gleiter, H. M., Haag, E., Shen, J. R., Eaton-Rye, J. J., Inoue, Y., Vermaas, W. F. J. & Renger, G. 1994. Functional characterization of mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 lacking short domains within the large, lumen-exposed loop of the chlorophyll-protein CP47 in photosystem II. - Biochemistry 33: 12063-12071.
    • (1994) Biochemistry , vol.33 , pp. 12063-12071
    • Gleiter, H.M.1    Haag, E.2    Shen, J.R.3    Eaton-Rye, J.J.4    Inoue, Y.5    Vermaas, W.F.J.6    Renger, G.7
  • 30
    • 0029053563 scopus 로고
    • Involvement of the CP47 protein in stabilization and photoactivation of a functional water oxidizing complex in the cyanobacterium Synechocystis sp. PCC6803
    • _, Haag, E., Shen, J.-R., Eaton-Rye, J. J., Seeliger, A. G., Inoue, Y., Vermaas, W. F. J. & Renger, G. 1995. Involvement of the CP47 protein in stabilization and photoactivation of a functional water oxidizing complex in the cyanobacterium Synechocystis sp. PCC6803. - Biochemistry 34: 6847-6856.
    • (1995) Biochemistry , vol.34 , pp. 6847-6856
    • Haag, E.1    Shen, J.-R.2    Eaton-Rye, J.J.3    Seeliger, A.G.4    Inoue, Y.5    Vermaas, W.F.J.6    Renger, G.7
  • 31
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • Gray, H. B. & Winkler, J. R. 1996. Electron transfer in proteins. - Annu. Rev. Biochem. 65: 537-561.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 32
    • 0027299939 scopus 로고
    • Functionally important domains of the large hydrophilic loop of CP 47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803
    • Haag, E., Eaton-Rye, J. J., Renger, G. & Vermaas, W. F. J. 1993. Functionally important domains of the large hydrophilic loop of CP 47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803. - Biochemistry 32: 4444-4454.
    • (1993) Biochemistry , vol.32 , pp. 4444-4454
    • Haag, E.1    Eaton-Rye, J.J.2    Renger, G.3    Vermaas, W.F.J.4
  • 33
    • 0026498102 scopus 로고
    • Proton transfer during the reaction between fully reduced cytochrome c oxidase and dioxygen: PH and deuterium isotope effects
    • Hallen, S. & Nilsson, T. 1992. Proton transfer during the reaction between fully reduced cytochrome c oxidase and dioxygen: pH and deuterium isotope effects. - Biochemistry 31: 11853-11859.
    • (1992) Biochemistry , vol.31 , pp. 11853-11859
    • Hallen, S.1    Nilsson, T.2
  • 35
    • 0000407944 scopus 로고    scopus 로고
    • Protons and charge indicators in oxygen evolution
    • D. R. Ort and C. F. Yocum, eds. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3683-6
    • Haumann, M. & Junge, W. 1996. Protons and charge indicators in oxygen evolution. - In Oxygenic Photosynthesis: The Light Reactions (D. R. Ort and C. F. Yocum, eds), pp. 165-192. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3683-6.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 165-192
    • Haumann, M.1    Junge, W.2
  • 36
    • 0002232564 scopus 로고
    • Oxygen evolution in photosynthesis
    • Govindjee, ed., Academic Press, New York, NY ISBN 0-12-294350-3
    • Joliot, P. & Kok, B. 1975. Oxygen evolution in photosynthesis. - In Bioenersetics of Photosynthesis (Govindjee, ed.), pp. 387-412. Academic Press, New York, NY ISBN 0-12-294350-3.
    • (1975) Bioenersetics of Photosynthesis , pp. 387-412
    • Joliot, P.1    Kok, B.2
  • 37
    • 0030046368 scopus 로고    scopus 로고
    • Effects of hydrogen/deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach
    • Karge, M., Irrgang, K.-D., Sellin, S., Feinäugle, R., Liu, B., Eckert, H.-J., Eichler, H. J. & Renger, G. 1996. Effects of hydrogen/deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach. - FEBS Lett. 378: 140-144.
    • (1996) FEBS Lett. , vol.378 , pp. 140-144
    • Karge, M.1    Irrgang, K.-D.2    Sellin, S.3    Feinäugle, R.4    Liu, B.5    Eckert, H.-J.6    Eichler, H.J.7    Renger, G.8
  • 41
    • 0011114276 scopus 로고
    • Temperature dependence of the S-state transition in a thermophilic cyanobacterium measured by thermoluminescence
    • J. Bigeins, ed., Martinus-Nijhoff, Dordrecht. ISBN 90-247-3450-9
    • Koike, H. & Inoue, Y. 1987. Temperature dependence of the S-state transition in a thermophilic cyanobacterium measured by thermoluminescence. - In Progress in Photosynthesis Research, Vol. I (J. Bigeins, ed.), pp. 645-648. Martinus-Nijhoff, Dordrecht. ISBN 90-247-3450-9.
    • (1987) Progress in Photosynthesis Research , vol.1 , pp. 645-648
    • Koike, H.1    Inoue, Y.2
  • 42
    • 0000575451 scopus 로고
    • Temperature dependence of S-state transition in a thermophilic cyanobacterium, Synechococcus vulcanus Copeland, measured by absorption changes in UV region
    • _, Hanssum, B., Inoue, Y. & Renger, G. 1987. Temperature dependence of S-state transition in a thermophilic cyanobacterium, Synechococcus vulcanus Copeland, measured by absorption changes in UV region. - Biochim. Biophys. Acta 893: 524-533.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 524-533
    • Hanssum, B.1    Inoue, Y.2    Renger, G.3
  • 43
    • 0029129548 scopus 로고
    • Evidence for the proximity of calcium to the manganese cluster of photosystem II: Determination by X-ray absorption spectroscopy
    • Latimer, M. J., DeRose, V. J., Mukerji, I., Yachandra, V. K., Sauer, K. & Klein, M. P. 1995. Evidence for the proximity of calcium to the manganese cluster of photosystem II: Determination by X-ray absorption spectroscopy. - Biochemistry 34: 10898-10909.
    • (1995) Biochemistry , vol.34 , pp. 10898-10909
    • Latimer, M.J.1    Derose, V.J.2    Mukerji, I.3    Yachandra, V.K.4    Sauer, K.5    Klein, M.P.6
  • 44
    • 0029805939 scopus 로고    scopus 로고
    • A one-site, two-state model for the binding of anions in photosystem II
    • Lindberg, K. & Andréasson, L.-E. 1996. A one-site, two-state model for the binding of anions in photosystem II. - Biochemistry 35: 14259-14267.
    • (1996) Biochemistry , vol.35 , pp. 14259-14267
    • Lindberg, K.1    Andréasson, L.-E.2
  • 45
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus, R. A. & Sutin, N. 1985. Electron transfer in chemistry and biology. - Biochim. Biophys. Acta 84: 265-322.
    • (1985) Biochim. Biophys. Acta , vol.84 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 46
    • 0025598137 scopus 로고
    • The reactivity of hydrazine with photosystem II strongly depends on the redox state of the water oxidizing system
    • Messinger, J. & Renger, G. 1990. The reactivity of hydrazine with photosystem II strongly depends on the redox state of the water oxidizing system. - FEBS Lett. 277: 141-146.
    • (1990) FEBS Lett. , vol.277 , pp. 141-146
    • Messinger, J.1    Renger, G.2
  • 47
    • 0027384113 scopus 로고
    • -2 of the water oxidase in isolated spinach thylakoids
    • -2 of the water oxidase in isolated spinach thylakoids. - Biochemistry 32: 9379-9386.
    • (1993) Biochemistry , vol.32 , pp. 9379-9386
    • Renger, G.1
  • 48
    • 0025946303 scopus 로고
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids. - Biochemistry 30: 7852-7862.
    • (1991) Biochemistry , vol.30 , pp. 7852-7862
    • Wacker, U.1    Renger, G.2
  • 49
    • 0027249446 scopus 로고
    • Structure-function relations in photosystem II. Effects of temperature and chaotropic agents on the period four oscillation of flash-induced oxygen evolution
    • _, Schröder, W. P. & Renger, G. 1993. Structure-function relations in photosystem II. Effects of temperature and chaotropic agents on the period four oscillation of flash-induced oxygen evolution. - Biochemistry 32: 7658-7668.
    • (1993) Biochemistry , vol.32 , pp. 7658-7668
    • Schröder, W.P.1    Renger, G.2
  • 52
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II
    • Michel, H. & Deisenhofer, J. 1988. Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II. - Biochemistry 27: 1-7.
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 54
    • 0029870735 scopus 로고    scopus 로고
    • Topology of core pigments and redox cofactors as inferred from electrochromic difference spectra
    • Mulkidjanian, A. Y., Cherepanov, D. A., Haumann, M. & Junge, W. 1996. Topology of core pigments and redox cofactors as inferred from electrochromic difference spectra. - Biochemistry 35: 3093-3107.
    • (1996) Biochemistry , vol.35 , pp. 3093-3107
    • Mulkidjanian, A.Y.1    Cherepanov, D.A.2    Haumann, M.3    Junge, W.4
  • 55
    • 0028948099 scopus 로고
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy. - Biochim. Biophys. Acta 1228: 189-200.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 189-200
    • Noguchi, T.1    Ono, T.2    Inoue, Y.3
  • 56
    • 0026685787 scopus 로고
    • X-ray detection of the period-four cycling of the manganese cluster in photosynthetic water oxidizing enzyme
    • Ono, T., Noguchi, T., Inoue, Y., Kusonoki, M., Matsushita, T. & Oyanagi, H. 1992. X-ray detection of the period-four cycling of the manganese cluster in photosynthetic water oxidizing enzyme. - Science 258: 1335-1337.
    • (1992) Science , vol.258 , pp. 1335-1337
    • Ono, T.1    Noguchi, T.2    Inoue, Y.3    Kusonoki, M.4    Matsushita, T.5    Oyanagi, H.6
  • 57
    • 0026587113 scopus 로고
    • Are there really four manganese per center of photosynthetic water oxidation?
    • Pauly, S. & Win, H. T. 1992. Are there really four manganese per center of photosynthetic water oxidation? - Biochim. Biophys. Acta 1099: 211-218.
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 211-218
    • Pauly, S.1    Win, H.T.2
  • 58
    • 0028344645 scopus 로고
    • Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex
    • Rappaport, F., Blanchard-Desce, M. & Lavergne, J. 1994. Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex. - Biochim. Biophys. Acta 1184: 178-192.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 178-192
    • Rappaport, F.1    Blanchard-Desce, M.2    Lavergne, J.3
  • 59
    • 0026654707 scopus 로고
    • Properties of iodide-activated photosynthetic water-oxidizing complexes
    • Rashid, A. & Homann, P. H. 1992. Properties of iodide-activated photosynthetic water-oxidizing complexes. - Biochim. Biophys. Acta 1101: 303-310.
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 303-310
    • Rashid, A.1    Homann, P.H.2
  • 60
    • 0010511574 scopus 로고
    • Theoretical studies about the functional and structural organization of photosynthetic oxygen evolution
    • H. Metzner, ed., Academic Press. London. ISBN 0-12-491750-X
    • Renger, G. 1978. Theoretical studies about the functional and structural organization of photosynthetic oxygen evolution. - In Photosynthetic Oxygen Evolution (H. Metzner, ed.), pp. 229-248. Academic Press. London. ISBN 0-12-491750-X.
    • (1978) Photosynthetic Oxygen Evolution , pp. 229-248
    • Renger, G.1
  • 61
    • 0345719573 scopus 로고
    • Biological energy conservation
    • Springer-Verlag, Berlin. ISBN 3-540-12083-1
    • _ 1983. Biological energy conservation. - In Biophysics (W. Hoppe, W. Lohmann, H. Markl and H. Ziegler, eds), pp. 347-371. Springer-Verlag, Berlin. ISBN 3-540-12083-1.
    • (1983) Biophysics , pp. 347-371
    • Hoppe, W.1    Lohmann, W.2    Markl, H.3    Ziegler, H.4
  • 62
    • 0001626228 scopus 로고
    • Mechanistic aspects of photosynthetic water cleavage
    • _ 1987. Mechanistic aspects of photosynthetic water cleavage. - Photosynthetica 21: 203-224.
    • (1987) Photosynthetica , vol.21 , pp. 203-224
  • 64
    • 0001558290 scopus 로고
    • Water cleavage by solar radiation - An inspiring challenge of photosynthesis research
    • _ 1993. Water cleavage by solar radiation - an inspiring challenge of photosynthesis research. - Photosynth. Res. 38: 229-247.
    • (1993) Photosynth. Res. , vol.38 , pp. 229-247
  • 65
    • 26744459326 scopus 로고    scopus 로고
    • Reaction center II and water oxidation in green plants
    • Birkhäuser, Basel. ISBN 3-7643-5295-7
    • _ 1997. Reaction center II and water oxidation in green plants. - In Treatise on Bioelectrochemistry, Bioenergetics, Vol. 4 (P. Gräber and G. Milazzo, eds), pp. 310-358. Birkhäuser, Basel. ISBN 3-7643-5295-7.
    • (1997) Treatise on Bioelectrochemistry, Bioenergetics , vol.4 , pp. 310-358
    • Gräber, P.1    Milazzo, G.2
  • 66
    • 0002769218 scopus 로고
    • The mechanism of photosynthetic water oxidation
    • - & Govindjee. 1985. The mechanism of photosynthetic water oxidation. - Photosynth. Res. 6: 33-55.
    • (1985) Photosynth. Res. , vol.6 , pp. 33-55
    • Govindjee1
  • 67
    • 0026566266 scopus 로고
    • Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach
    • - & Hanssum, B. 1992. Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach. - FEBS Lett. 299: 28-32.
    • (1992) FEBS Lett. , vol.299 , pp. 28-32
    • Hanssum, B.1
  • 68
    • 0000765461 scopus 로고
    • Studies on the proton release of the donor side of system II. Correlation between oxidation and deprotonization of donor D1 in Tris-washed inside-out thylakoids
    • - & Völker, M. 1982. Studies on the proton release of the donor side of system II. Correlation between oxidation and deprotonization of donor D1 in Tris-washed inside-out thylakoids. - FEBS Lett. 149: 203-207.
    • (1982) FEBS Lett. , vol.149 , pp. 203-207
    • Völker, M.1
  • 69
    • 0028362937 scopus 로고
    • Structure-function relationship in photosynthetic water oxidation
    • _, Bittner, T. & Messinger, J. 1994. Structure-function relationship in photosynthetic water oxidation. - Biochem. Soc. Trans. 22: 318-322.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 318-322
    • Bittner, T.1    Messinger, J.2
  • 70
    • 15844409181 scopus 로고    scopus 로고
    • Reduced derivatives of the Mn cluster in the oxygen-evolving complex of photosystem II: An EXAFS study
    • Riggs-Gelasco, P. J., Mei, R., Yocum, C. F. & Penner-Hahn, J. E. 1996a. Reduced derivatives of the Mn cluster in the oxygen-evolving complex of photosystem II: An EXAFS study. - J. Am. Chem. Soc. 118: 2387-2399.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2387-2399
    • Riggs-Gelasco, P.J.1    Mei, R.2    Yocum, C.F.3    Penner-Hahn, J.E.4
  • 71
    • 0030110871 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of calcium-substituted derivatives of the oxygen-evolving complex of photosystem II
    • _, Mei, R., Ghanotakis, D. F., Yocum, C. F. & Penner-Hahn, J. E. 1996b. X-ray absorption spectroscopy of calcium-substituted derivatives of the oxygen-evolving complex of photosystem II. - J. Am. Chem. Soc. 118: 2400-2410.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2400-2410
    • Mei, R.1    Ghanotakis, D.F.2    Yocum, C.F.3    Penner-Hahn, J.E.4
  • 75
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of photosystem II
    • Seidler, A. 1996. The extrinsic polypeptides of photosystem II. - Biochim. Biophys. Acta 1277: 35-60.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 76
    • 0028960117 scopus 로고
    • The role of cytochrome c550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803
    • Shen, J.-R., Vermaas, W. J. F. & Inoue, Y. 1995. The role of cytochrome c550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803. - J. Biol. Chem. 270: 6901-6907.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6901-6907
    • Shen, J.-R.1    Vermaas, W.J.F.2    Inoue, Y.3
  • 77
    • 45949125703 scopus 로고
    • Photoactivation of the water-oxidizing complex in photosystem II membranes depleted of Mn and extrinsic proteins
    • Tamura, N. & Cheniae, G. 1987. Photoactivation of the water-oxidizing complex in photosystem II membranes depleted of Mn and extrinsic proteins. - Biochim. Biophys. Acta 890: 179-197.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 179-197
    • Tamura, N.1    Cheniae, G.2
  • 79
    • 0001052784 scopus 로고
    • 2 state multiline signal in the thermophilic cyanobacterium Synechococcus elongatus
    • 2 state multiline signal in the thermophilic cyanobacterium Synechococcus elongatus. - J. Am. Chem. Soc. 115: 2382-2389.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 2382-2389
    • Tang, X.S.1    Sivaraja, M.2    Dismukes, G.C.3
  • 80
    • 0027979782 scopus 로고
    • Identification of histidine at the catalytic site of the photosynthetic oxygen-evolving complex
    • _, Diner, B. A., Larsen, B. S., Gilchrist, M. L., Lorigan, G. A. & Britt, R. D. 1994. Identification of histidine at the catalytic site of the photosynthetic oxygen-evolving complex. - Proc. Natl. Acad. Sci. USA 91: 704-708.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 704-708
    • Diner, B.A.1    Larsen, B.S.2    Gilchrist, M.L.3    Lorigan, G.A.4    Britt, R.D.5
  • 81
    • 0025815921 scopus 로고
    • Calcium limits substrate accessibility or reactivity at the manganese cluster in photosynthetic water oxidation
    • Tso, J., Sivaraja, M. & Dismukes, G. C. 1991. Calcium limits substrate accessibility or reactivity at the manganese cluster in photosynthetic water oxidation. - Biochemistry 30: 4734-4739.
    • (1991) Biochemistry , vol.30 , pp. 4734-4739
    • Tso, J.1    Sivaraja, M.2    Dismukes, G.C.3
  • 82
    • 0028283983 scopus 로고
    • Angular orientation of the stable tyrosyl radical within photosystem II by high-field 245-GHz electron paramagnetic resonance
    • Un, S., Brunel, L.-C., Brill, T. M., Zimmermann, J.-L. & Rutherford, A. W. 1994. Angular orientation of the stable tyrosyl radical within photosystem II by high-field 245-GHz electron paramagnetic resonance. - Proc. Natl. Acad. Sci. USA 91: 5262-5266.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5262-5266
    • Un, S.1    Brunel, L.-C.2    Brill, T.M.3    Zimmermann, J.-L.4    Rutherford, A.W.5
  • 83
    • 0000960124 scopus 로고
    • Kok's oxygen clock: What makes it tick? the structure of P680 and consequences of its oxidizing power
    • van Gorkom, H. J. & Schelvis, J. P. M. 1993. Kok's oxygen clock: What makes it tick? The structure of P680 and consequences of its oxidizing power. - Photosynth. Res. 38: 297-301.
    • (1993) Photosynth. Res. , vol.38 , pp. 297-301
    • Van Gorkom, H.J.1    Schelvis, J.P.M.2
  • 85
    • 0026096798 scopus 로고
    • H dependent charge equilibria between tyrosine D and the S-states in photosystem II. Estimation of relative midpoint redox potentials
    • Vass, I. & Styring, S. 1991. pH dependent charge equilibria between tyrosine D and the S-states in photosystem II. Estimation of relative midpoint redox potentials. - Biochemistry 30: 830-839.
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 87
    • 0026067824 scopus 로고
    • An electroluminescence study of stabilization reactions in the oxygen-evolving complex of photosystem II
    • Vos, M. H., van Gorkom, H, J. & van Leeuwen, P. J. 1991. An electroluminescence study of stabilization reactions in the oxygen-evolving complex of photosystem II. - Biochim. Biophys. Acta 1056: 27-39.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 27-39
    • Vos, M.H.1    Van Gorkom, H.J.2    Van Leeuwen, P.J.3
  • 88
    • 0002266330 scopus 로고
    • Is there a direct chloride cofactor requirement in the oxygen-evolving reactions of photosystem II
    • Wydrzynski, T., Baumgart, F., MacMillan, F. & Renger, G. 1990. Is there a direct chloride cofactor requirement in the oxygen-evolving reactions of photosystem II. - Photosynth. Res. 25: 59-72.
    • (1990) Photosynth. Res. , vol.25 , pp. 59-72
    • Wydrzynski, T.1    Baumgart, F.2    MacMillan, F.3    Renger, G.4
  • 89
    • 0027173103 scopus 로고
    • Where plants make oxygen: A structural model for the photosynthetic oxygen-evolving manganese cluster
    • Yachandra, V K., DeRose, V. J., Latimer, M. J., Mukerji, I., Sauer, K. & Klein, M. P. 1993. Where plants make oxygen: A structural model for the photosynthetic oxygen-evolving manganese cluster. - Science 260: 675-679.
    • (1993) Science , vol.260 , pp. 675-679
    • Yachandra, V.K.1    DeRose, V.J.2    Latimer, M.J.3    Mukerji, I.4    Sauer, K.5    Klein, M.P.6
  • 90
    • 0040070502 scopus 로고    scopus 로고
    • Manganese cluster in photosynthesis. Where plants oxidize water to dioxygen
    • Yachandra, V. K., Sauer, K. & Klein, M. P. 1996. Manganese cluster in photosynthesis. Where plants oxidize water to dioxygen. - Chem. Rev. 96: 2927-2950.
    • (1996) Chem. Rev. , vol.96 , pp. 2927-2950
    • Yachandra, V.K.1    Sauer, K.2    Klein, M.P.3
  • 91
    • 0002283325 scopus 로고
    • The calcium and chloride requirements for photosynthetic water oxidation
    • V. L. Pecoraro, ed., VCH, New York, NY. ISBN 0-89573-729-9
    • Yocum, C. F. 1992. The calcium and chloride requirements for photosynthetic water oxidation. - In Manganese Redox Enzymes (V. L. Pecoraro, ed.), pp. 71-83. VCH, New York, NY. ISBN 0-89573-729-9.
    • (1992) Manganese Redox Enzymes , pp. 71-83
    • Yocum, C.F.1
  • 93
    • 0343224870 scopus 로고
    • EPR and ENDOR studies of manganese clusters in the water oxidizing complex and related modes compounds
    • N. Murata, ed., Kluwer, Dordrecht. ISBN 0-7923-2091-3
    • Zweygart, W., Weyhermuller, T., Renger, G., Wieghardt, K. & Lubitz, W. 1992. EPR and ENDOR studies of manganese clusters in the water oxidizing complex and related modes compounds. - In Research in Photosynthesis (N. Murata, ed.), Vol. 2, pp. 289-292. Kluwer, Dordrecht. ISBN 0-7923-2091-3.
    • (1992) Research in Photosynthesis , vol.2 , pp. 289-292
    • Zweygart, W.1    Weyhermuller, T.2    Renger, G.3    Wieghardt, K.4    Lubitz, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.