메뉴 건너뛰기




Volumn 357, Issue 1426, 2002, Pages 1395-1405

Water oxidation chemistry of photosystem II

Author keywords

Calcium; Chloride; Manganese; Oxygen evolving complex; Photosystem II; Tyrosyl radical

Indexed keywords

OXIDATION; PHOTOSYNTHESIS; WATER;

EID: 0037195338     PISSN: 09628436     EISSN: None     Source Type: Journal    
DOI: 10.1098/rstb.2002.1136     Document Type: Conference Paper
Times cited : (50)

References (89)
  • 1
    • 0001059402 scopus 로고
    • Oxidation of thioanisoles and methyl phenyl sulfides by oxo(phosphine)ruthenium(IV) complexes
    • Acquaye, J. H., Muller, J. G. & Takeuchi, K. J. 1993 Oxidation of thioanisoles and methyl phenyl sulfides by oxo(phosphine)ruthenium(IV) complexes. Inorg. Chem. 32, 160-165.
    • (1993) Inorg. Chem. , vol.32 , pp. 160-165
    • Acquaye, J.H.1    Muller, J.G.2    Takeuchi, K.J.3
  • 2
    • 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, 155-164.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andréasson, L.-E.1    Vass, I.2    Styring, S.3
  • 3
    • 0002666492 scopus 로고
    • Reduction potentials of various haemerythrin oxidation states
    • Armstrong, F. A., Harrington, P. C. & Wilkins, R. G. 1983 Reduction potentials of various haemerythrin oxidation states. J. Inorg. Biochem. 18, 83-91.
    • (1983) J. Inorg. Biochem. , vol.18 , pp. 83-91
    • Armstrong, F.A.1    Harrington, P.C.2    Wilkins, R.G.3
  • 4
    • 0034673314 scopus 로고    scopus 로고
    • Hydrogen atom abstraction by metal-oxo and metal-superoxo complexes: Kinetics and thermodynamics
    • Bakac, A. 2000 Hydrogen atom abstraction by metal-oxo and metal-superoxo complexes: Kinetics and thermodynamics. J. Am. Chem. Soc. 122, 1092-1097.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1092-1097
    • Bakac, A.1
  • 5
    • 0002878472 scopus 로고    scopus 로고
    • 'Oxo-hydroxo tautomerism' as a useful mechanistic tool in oxygenations catalysed by water soluble metalloporphyrins
    • Bernadou, J. & Meunier, B. 1998 'Oxo-hydroxo tautomerism' as a useful mechanistic tool in oxygenations catalysed by water soluble metalloporphyrins. J. Chem. Soc. Chem. Comm. 2167-2173.
    • (1998) J. Chem. Soc. Chem. Comm. , pp. 2167-2173
    • Bernadou, J.1    Meunier, B.2
  • 6
    • 0001346223 scopus 로고
    • 'Redox tautomerism' in high-valent metal-oxo-aqua complexes. Origin of oxygen atom in epoxidation reactions catalysed by water-soluble metalloporphyrins
    • Bernadou, J., Fabiano, A.-S., Robert, A. & Meunier, B. 1994 'Redox tautomerism' in high-valent metal-oxo-aqua complexes. Origin of oxygen atom in epoxidation reactions catalysed by water-soluble metalloporphyrins. J. Am. Chem. Soc. 116, 9375-9376.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9375-9376
    • Bernadou, J.1    Fabiano, A.-S.2    Robert, A.3    Meunier, B.4
  • 7
    • 0032575361 scopus 로고    scopus 로고
    • Hydrogen bonding of redox-active tyrosine Z of photosystem II probed by FTIR difference spectroscopy
    • Berthomieu, C., Hienerwadel, R., Boussac, A., Breton, J. & Diner, B. A. 1998 Hydrogen bonding of redox-active tyrosine Z of photosystem II probed by FTIR difference spectroscopy. Biochemistry 37, 10 547-10 554.
    • (1998) Biochemistry , vol.37 , pp. 10547-10554
    • Berthomieu, C.1    Hienerwadel, R.2    Boussac, A.3    Breton, J.4    Diner, B.A.5
  • 8
    • 0029165797 scopus 로고
    • Rapid proton-transfer under flashing light at both functional sides of dark-adapted photosystem II particles
    • Bögershausen, O. & Junge, W. 1995 Rapid proton-transfer under flashing light at both functional sides of dark-adapted photosystem II particles. Biochim. Biophys. Acta 1230, 177-185.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 177-185
    • Bögershausen, O.1    Junge, W.2
  • 10
    • 0000161895 scopus 로고
    • Substituent effects on the stabilities of phenoxyl radicals and the acidities of phenoxyl radical cations
    • Bordwell, F. G. & Cheng, J.-P. 1991 Substituent effects on the stabilities of phenoxyl radicals and the acidities of phenoxyl radical cations. J. Am. Chem. Soc. 113, 1736-1743.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1736-1743
    • Bordwell, F.G.1    Cheng, J.-P.2
  • 11
    • 0034517606 scopus 로고    scopus 로고
    • Zinc/calcium- and cadmium/cadmium-substituted concanavalin A: Interplay of metal binding, pH and molecular packing
    • Bouckaert, J., Loris, R. & Wyns, L. 2000 Zinc/calcium- and cadmium/cadmium-substituted concanavalin A: interplay of metal binding, pH and molecular packing. Acta Cryst. D 56, 1569-1576.
    • (2000) Acta Cryst. D , vol.56 , pp. 1569-1576
    • Bouckaert, J.1    Loris, R.2    Wyns, L.3
  • 14
    • 0000561603 scopus 로고    scopus 로고
    • Oxygen evolution
    • ed. D. R. Ort & C. F. Yocum. Dordrecht, The Netherlands: Kluwer
    • Britt, R. D. 1996 Oxygen evolution. In Oxygenic Photosynthesis: The Light Reactions, vol. 4 (ed. D. R. Ort & C. F. Yocum), pp. 137-159. Dordrecht, The Netherlands: Kluwer.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , vol.4 , pp. 137-159
    • Britt, R.D.1
  • 15
    • 0000269978 scopus 로고
    • The effect of temperature on the formation and decay of the multiline EPR signal species associated with photosynthetic oxygen evolution
    • Brudvig, G. W., Casey, J. L. & Sauer, K. 1983 The effect of temperature on the formation and decay of the multiline EPR signal species associated with photosynthetic oxygen evolution. Biochim. Biophys. Acta 723, 366-371.
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 366-371
    • Brudvig, G.W.1    Casey, J.L.2    Sauer, K.3
  • 16
    • 38049048527 scopus 로고
    • Electron paramagnetic resonance detection of a cryogenically photogenerated intermediate in photosynthetic oxygen evolution
    • Casey, J. L. & Sauer, K. 1984 Electron paramagnetic resonance detection of a cryogenically photogenerated intermediate in photosynthetic oxygen evolution. Biochim. Biophys. Acta 767, 21-28.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 21-28
    • Casey, J.L.1    Sauer, K.2
  • 17
    • 0030956950 scopus 로고    scopus 로고
    • Thermodynamic viability of hydrogen atom transfer from water coordinated to the oxygen-evolving complex of photosystem II
    • Caudle, M. T. & Pecoraro, V. L. 1997 Thermodynamic viability of hydrogen atom transfer from water coordinated to the oxygen-evolving complex of photosystem II. J. Am. Chem. Soc. 119, 3415-3416.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3415-3416
    • Caudle, M.T.1    Pecoraro, V.L.2
  • 18
    • 0033573843 scopus 로고    scopus 로고
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects. Biochemistry 38, 2068-2077.
    • (1999) Biochemistry , vol.38 , pp. 2068-2077
    • Christen, G.1    Renger, G.2
  • 19
    • 0033545726 scopus 로고    scopus 로고
    • +· reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids
    • +· reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids. Biochemistry 38, 6082-6092.
    • (1999) Biochemistry , vol.38 , pp. 6082-6092
    • Christen, G.1    Seeliger, A.2    Renger, G.3
  • 20
    • 0029033834 scopus 로고
    • Amino acid residues that influence the binding of manganese or calcium to photosystem II. 1. The lumenal interhelical domains of the D1 polypeptide
    • 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 lumenal 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
  • 21
    • 0029071492 scopus 로고
    • Amino acid residues that influence the binding of manganese or calcium to photosystem II. 2. The carboxy-terminal domain of the D1 polypeptide
    • Chu, H.-A., Nguyen, A.-P. & Debus, R. J. 1995b Amino acid residues that influence the binding of manganese or calcium to photosystem II. 2. The carboxy-terminal domain of the D1 polypeptide. Biochemistry 34, 5859-5882.
    • (1995) Biochemistry , vol.34 , pp. 5859-5882
    • Chu, H.-A.1    Nguyen, A.-P.2    Debus, R.J.3
  • 22
    • 0032234424 scopus 로고    scopus 로고
    • Proton-coupled electron transfer
    • Cukier, R. I. & Nocera, D. G. 1998 Proton-coupled electron transfer. A. Rev. Phys. Chem. 49, 337-369.
    • (1998) A. Rev. Phys. Chem. , vol.49 , pp. 337-369
    • Cukier, R.I.1    Nocera, D.G.2
  • 24
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • Debus, R. J. 1992 The manganese and calcium ions of photosynthetic oxygen evolution. Biochim. Biophys. Acta 1102, 269-352.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 29
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • Falke, J. J., Drake, S. K., Hazard, A. L. & Peersen, O. B. 1994 Molecular tuning of ion binding to calcium signaling proteins. Q. Rev. Biophys. 27, 219-290.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 30
    • 0040999286 scopus 로고
    • Catalytic oxidation of water by an oxo-bridged ruthenium dimer
    • Gersten, S. W., Samuels, G. J. & Meyer, T. J. 1982 Catalytic oxidation of water by an oxo-bridged ruthenium dimer. J. Am. Chem. Soc. 104, 4029-4030.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4029-4030
    • Gersten, S.W.1    Samuels, G.J.2    Meyer, T.J.3
  • 31
    • 0000981541 scopus 로고
    • Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations
    • Ghanotakis, D. F., Babcock, G. T. & Yocum, C. F. 1984 Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations. FEBS Lett. 167, 127-130.
    • (1984) FEBS Lett. , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 32
    • 33845282746 scopus 로고
    • Olefin epoxidation by manganese(IV) porphyrins: Evidence for two reaction pathways
    • Groves, J. T. & Stern, M. K. 1987 Olefin epoxidation by manganese(IV) porphyrins: Evidence for two reaction pathways. J. Am. Chem. Soc. 109, 3812-3814.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3812-3814
    • Groves, J.T.1    Stern, M.K.2
  • 33
    • 0000645586 scopus 로고
    • Synthesis, characterization, and reactivity of oxomanganese(IV) porphyrin complexes
    • Groves, J. T. & Stern, M. K. 1988 Synthesis, characterization, and reactivity of oxomanganese(IV) porphyrin complexes. J. Am. Chem. Soc. 110, 8628-8638.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8628-8638
    • Groves, J.T.1    Stern, M.K.2
  • 34
    • 0030804770 scopus 로고    scopus 로고
    • Detection and characterization of an oxomanganese(V) porphyrin complex by rapid-mixing stopped-flow spectrophotometry
    • Groves, J. T., Lee, J. & Marla, S. S. 1997 Detection and characterization of an oxomanganese(V) porphyrin complex by rapid-mixing stopped-flow spectrophotometry. J. Am. Chem. Soc. 119, 6269-6273.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6269-6273
    • Groves, J.T.1    Lee, J.2    Marla, S.S.3
  • 36
    • 0030970415 scopus 로고    scopus 로고
    • Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of photosystem II
    • Haumann, M., Bögershausen, O., Cherepanov, D., Ahlbrink, R. & Junge, W. 1997 Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of photosystem II. Photosynth. Res. 51, 193-208.
    • (1997) Photosynth. Res. , vol.51 , pp. 193-208
    • Haumann, M.1    Bögershausen, O.2    Cherepanov, D.3    Ahlbrink, R.4    Junge, W.5
  • 37
    • 0032508393 scopus 로고    scopus 로고
    • Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study
    • Hays, A.-M. A., Vassiliev, I. R., Golbeck, J. H. & Debus, R. J. 1998 Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study. Biochemistry 37, 11 352-11 365.
    • (1998) Biochemistry , vol.37 , pp. 11352-11365
    • Hays, A.-M.A.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 39
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • Hoganson, C. W. & Babcock, G. T. 1997 A metalloradical mechanism for the generation of oxygen from water in photosynthesis. Science 277, 1953-1956.
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 41
    • 0002232564 scopus 로고
    • Oxygen evolution in photosynthesis
    • (ed. Govindjee), New York: Academic
    • Joliot, P. & Kok, B. 1975 Oxygen evolution in photosynthesis. In Bioenergetics of Photosynthesis (ed. Govindjee), pp. 387-412. New York: Academic.
    • (1975) Bioenergetics of Photosynthesis , pp. 387-412
    • Joliot, P.1    Kok, B.2
  • 42
    • 0006881932 scopus 로고
    • On the proximal effect of the nitrogen ligands on the oxomanganese porphyrin system
    • Jørgensen, K. A. & Swanstrøm, P. 1988 On the proximal effect of the nitrogen ligands on the oxomanganese porphyrin system. Acta Chem. Scand. 43, 822-824.
    • (1988) Acta Chem. Scand. , vol.43 , pp. 822-824
    • Jørgensen, K.A.1    Swanstrøm, P.2
  • 44
    • 0000575451 scopus 로고
    • Temperature dependence of S-state transition in a thermophilic cyanobacterium, Synechococcus vulcanus Copeland measured by absorption changes in the ultraviolet region
    • Koike, H., 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 the ultraviolet region. Biochim. Biophys. Acta 893, 524-533.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 524-533
    • Koike, H.1    Hanssum, B.2    Inoue, Y.3    Renger, G.4
  • 46
    • 0029951409 scopus 로고    scopus 로고
    • Net charge oscillation and proton release during water oxidation in photosynthesis. An electrochromic band shift study at pH 5.5-7.0
    • Kretschmann, H., Schlodder, E. & Witt, H. T. 1996 Net charge oscillation and proton release during water oxidation in photosynthesis. An electrochromic band shift study at pH 5.5-7.0. Biochim. Biophys. Acta 1274, 1-8.
    • (1996) Biochim. Biophys. Acta , vol.1274 , pp. 1-8
    • Kretschmann, H.1    Schlodder, E.2    Witt, H.T.3
  • 47
    • 0037158924 scopus 로고    scopus 로고
    • Proton-coupled electron transfer involving tyrosine Z in photosystem II
    • Kühne, H. & Brudvig, G. W. 2002 Proton-coupled electron transfer involving tyrosine Z in photosystem II. J. Phys. Chem. B 106, 8189-8196.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 8189-8196
    • Kühne, H.1    Brudvig, G.W.2
  • 48
    • 0037798468 scopus 로고    scopus 로고
    • Competitive binding of chloride and acetate in photosystem II
    • Kühne, H., Szalai, V. A. & Brudvig, G. W. 1999 Competitive binding of chloride and acetate in photosystem II. Biochemistry 38, 6604-6613.
    • (1999) Biochemistry , vol.38 , pp. 6604-6613
    • Kühne, H.1    Szalai, V.A.2    Brudvig, G.W.3
  • 51
    • 0001740481 scopus 로고
    • Proton release during the redox cycle of the water oxidase
    • Lavergne, J. & Junge, W. 1993 Proton release during the redox cycle of the water oxidase. Photosynth. Res. 38, 279-296.
    • (1993) Photosynth. Res. , vol.38 , pp. 279-296
    • Lavergne, J.1    Junge, W.2
  • 52
    • 0030889141 scopus 로고    scopus 로고
    • 2 evolution and permanganate formation from high-valent manganese complexes
    • 2 evolution and permanganate formation from high-valent manganese complexes. J. Am. Chem. Soc. 119, 2761-2762.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2761-2762
    • Limburg, J.1    Brudvig, G.W.2    Crabtree, R.H.3
  • 56
    • 0026409654 scopus 로고
    • Calcium-binding sites in proteins: A structural perspective
    • McPhalen, C. A., Strynadka, N. C. J. & James, M. N. G. 1991 Calcium-binding sites in proteins: A structural perspective. Adv. Protein Chem. 42, 77-144.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 77-144
    • McPhalen, C.A.1    Strynadka, N.C.J.2    James, M.N.G.3
  • 57
    • 0032491189 scopus 로고    scopus 로고
    • Involvement of histidine 190 on the D1 protein in electron/proton transfer reactions on the donor side of photosystem II
    • Mamedov, F., Sayre, R. T. & Styring, S. 1998 Involvement of histidine 190 on the D1 protein in electron/proton transfer reactions on the donor side of photosystem II. Biochemistry 37, 14 245-14 256.
    • (1998) Biochemistry , vol.37 , pp. 14245-14256
    • Mamedov, F.1    Sayre, R.T.2    Styring, S.3
  • 58
    • 0000647193 scopus 로고    scopus 로고
    • Hydrogen atom abstraction by metal-oxo complexes: Understanding the analogy with organic radical reactions
    • Mayer, J. M. 1998 Hydrogen atom abstraction by metal-oxo complexes: Understanding the analogy with organic radical reactions. Accts Chem. Res. 31, 441-450.
    • (1998) Accts Chem. Res. , vol.31 , pp. 441-450
    • Mayer, J.M.1
  • 59
    • 33845278658 scopus 로고
    • Proximal effect of the nitrogen ligands in the catalytic epoxidation of olefins by the NaOCl/manganese(III) porphyrin system
    • Meunier, B., Decarvalho, M. E., Bortolini, O. & Momenteau, M. 1988 Proximal effect of the nitrogen ligands in the catalytic epoxidation of olefins by the NaOCl/manganese(III) porphyrin system. Inorg. Chem. 27, 161-164.
    • (1988) Inorg. Chem. , vol.27 , pp. 161-164
    • Meunier, B.1    Decarvalho, M.E.2    Bortolini, O.3    Momenteau, M.4
  • 60
    • 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
  • 61
    • 0026569892 scopus 로고
    • Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster
    • Nixon, P. J. & Diner, B. A. 1992 Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster. Biochemistry 31, 942-948.
    • (1992) Biochemistry , vol.31 , pp. 942-948
    • Nixon, P.J.1    Diner, B.A.2
  • 62
    • 0030832914 scopus 로고    scopus 로고
    • Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by Fourier transform infrared spectroscopy
    • Noguchi, T., Inoue, Y. & Tang, X.-S. 1997 Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by Fourier transform infrared spectroscopy. Biochemistry 36, 14 705-14 711.
    • (1997) Biochemistry , vol.36 , pp. 14705-14711
    • Noguchi, T.1    Inoue, Y.2    Tang, X.-S.3
  • 63
    • 0001617374 scopus 로고
    • 2-washed PS II particles depleted of 33, 24 and 16 kDa proteins
    • 2-washed PS II particles depleted of 33, 24 and 16 kDa proteins. FEBS Lett. 168, 281-286.
    • (1984) FEBS Lett. , vol.168 , pp. 281-286
    • Ono, T.1    Inoue, Y.2
  • 65
    • 0032527668 scopus 로고    scopus 로고
    • 55Mn pulsed ENDOR demonstrates that the photosystem II 'split' EPR signal arises from a magnetically-coupled manganotyrosyl complex
    • 55Mn pulsed ENDOR demonstrates that the photosystem II 'split' EPR signal arises from a magnetically-coupled manganotyrosyl complex. J. Am. Chem. Soc. 120, 6840-6841.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6840-6841
    • Peloquin, J.M.1    Campbell, K.A.2    Britt, R.D.3
  • 67
    • 0030660560 scopus 로고    scopus 로고
    • Charge recombination and proton transfer in manganese-depleted photosystem II
    • Rappaport, F. & Lavergne, J. 1997 Charge recombination and proton transfer in manganese-depleted photosystem II. Biochemistry 36, 15 294-15 302.
    • (1997) Biochemistry , vol.36 , pp. 15294-15302
    • Rappaport, F.1    Lavergne, J.2
  • 68
    • 0000765461 scopus 로고
    • Studies on the proton release pattern of the donor side of system 2. Correlation between oxidation and deprotonization of donor D1 in tris-washed inside-out thylakoids
    • Renger, G. & Völker, M. 1982 Studies on the proton release pattern of the donor side of system 2. 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
    • Renger, G.1    Völker, M.2
  • 69
    • 0030110871 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of calcium-substituted derivatives of the oxygen-evolving complex of photosystem II
    • Riggs-Gelasco, P. J., Mei, R., Ghanotakis, D. F., Yocum, C. F. & Penner-Hahn, J. E. 1996 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
    • Riggs-Gelasco, P.J.1    Mei, R.2    Ghanotakis, D.F.3    Yocum, C.F.4    Penner-Hahn, J.E.5
  • 71
    • 0033550515 scopus 로고    scopus 로고
    • Manganese oxyl radical intermediates and O-O bond formation in photosynthetic oxygen evolution and a proposed role for the calcium cofactor in photosystem II
    • Siegbahn, P. E. M. & Crabtree, R. H. 1999 Manganese oxyl radical intermediates and O-O bond formation in photosynthetic oxygen evolution and a proposed role for the calcium cofactor in photosystem II. J. Am. Chem. Soc. 121, 117-127.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 117-127
    • Siegbahn, P.E.M.1    Crabtree, R.H.2
  • 73
    • 0001404648 scopus 로고
    • Deactivation kinetics and temperature dependence of the S-state transitions in the oxygen-evolving system of photosystem II measured by EPR spectroscopy
    • Styring, S. & Rutherford, A. W. 1988 Deactivation kinetics and temperature dependence of the S-state transitions in the oxygen-evolving system of photosystem II measured by EPR spectroscopy. Biochim. Biophys. Acta 933, 378-387.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 378-387
    • Styring, S.1    Rutherford, A.W.2
  • 74
    • 0030473275 scopus 로고    scopus 로고
    • Reversible binding of nitric oxide to tyrosyl radicals in photosystem II. Nitric oxide quenches formation of the S3 EPR signal species in acetate-inhibited photosystem II
    • Szalai, V. A. & Brudvig, G. W. 1996 Reversible binding of nitric oxide to tyrosyl radicals in photosystem II. Nitric oxide quenches formation of the S3 EPR signal species in acetate-inhibited photosystem II. Biochemistry 35, 15 080-15 087.
    • (1996) Biochemistry , vol.35 , pp. 15080-15087
    • Szalai, V.A.1    Brudvig, G.W.2
  • 75
    • 0344074652 scopus 로고    scopus 로고
    • Characterization of the interaction between manganese and tyrosine Z in acetate-inhibited photosystem II
    • Szalai, V. A., Kühne, H., Lakshmi, K. V. & Brudvig, G. W. 1998a Characterization of the interaction between manganese and tyrosine Z in acetate-inhibited photosystem II. Biochemistry 37, 13 594-13 603.
    • (1998) Biochemistry , vol.37 , pp. 13594-13603
    • Szalai, V.A.1    Kühne, H.2    Lakshmi, K.V.3    Brudvig, G.W.4
  • 77
    • 0029760320 scopus 로고    scopus 로고
    • Manganese-tyrosine interaction in the photosystem II oxygen-evolving complex
    • Tang, X.-S., Randall, D. W., Force, D. A., Diner, B. A. & Britt, R. D. 1996a Manganese-tyrosine interaction in the photosystem II oxygen-evolving complex. J. Am. Chem. Soc. 118, 7638-7639.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7638-7639
    • Tang, X.-S.1    Randall, D.W.2    Force, D.A.3    Diner, B.A.4    Britt, R.D.5
  • 81
    • 0035808638 scopus 로고    scopus 로고
    • Mechanism of photosynthetic water oxidation: Combining biophysical studies of photosystem II with inorganic model chemistry
    • Vrettos, J. S., Limburg, J. & Brudvig, G. W. 2001a Mechanism of photosynthetic water oxidation: Combining biophysical studies of photosystem II with inorganic model chemistry. Biochim. Biophys. Acta 1503, 229-245.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 229-245
    • Vrettos, J.S.1    Limburg, J.2    Brudvig, G.W.3
  • 86
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • Wood, P. M. 1988 The potential diagram for oxygen at pH 7. Biochem. J. 253, 287-289.
    • (1988) Biochem. J. , vol.253 , pp. 287-289
    • Wood, P.M.1
  • 87
    • 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
  • 88
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauß, N., Saenger, W. & Orth, P. 2001 Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739-743.
    • (2001) Nature , vol.409 , 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
  • 89
    • 0028829367 scopus 로고
    • Isolation and characterization of a photosystem II complex from the red alga Cyanidium caldarium: Association of cytochrome c-550 and 12 kDA protein with the complex
    • Enami, I., Murayama, H., Onta, 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 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    Onta, H.3    Kamo, M.4    Nakazato, K.5    Shen, J.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.