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Volumn 1655, Issue 1-3, 2004, Pages 222-230

The stable tyrosyl radical in Photosystem II: Why D?

Author keywords

G.T. Babcock; Photosystem II; Redox reaction; Tyrosine D; Tyrosyl radical

Indexed keywords

CHLOROPHYLL; MANGANESE; OXIDIZING AGENT; PHOSPHORUS; TYROSINE;

EID: 1942440387     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.10.016     Document Type: Review
Times cited : (96)

References (74)
  • 1
    • 0015760626 scopus 로고
    • Electron paramagnetic resonance signal II in spinach chloroplast. I. Kinetic analysis for untreated chloroplasts
    • Babcock G.T., Sauer K. Electron paramagnetic resonance signal II in spinach chloroplast. I. Kinetic analysis for untreated chloroplasts. Biochim. Biophys. Acta. 325:1973;483-503.
    • (1973) Biochim. Biophys. Acta , vol.325 , pp. 483-503
    • Babcock, G.T.1    Sauer, K.2
  • 2
    • 0016429902 scopus 로고
    • A rapid, light-induced transient in electron paramagnetic resonance signal II activated upon inhibition of photosynthetic oxygen evolution
    • Babcock G.T., Sauer K. A rapid, light-induced transient in electron paramagnetic resonance signal II activated upon inhibition of photosynthetic oxygen evolution. Biochim. Biophys. Acta. 376:1975;315-328.
    • (1975) Biochim. Biophys. Acta , vol.376 , pp. 315-328
    • Babcock, G.T.1    Sauer, K.2
  • 3
    • 0016433801 scopus 로고
    • The rapid component of electron paramagnetic resonance signal II: A candidate for the physiological donor to Photosystem II in spinach chloroplasts
    • Babcock G.T., Sauer K. The rapid component of electron paramagnetic resonance signal II: a candidate for the physiological donor to Photosystem II in spinach chloroplasts. Biochim. Biophys. Acta. 376:1975;329-344.
    • (1975) Biochim. Biophys. Acta , vol.376 , pp. 329-344
    • Babcock, G.T.1    Sauer, K.2
  • 4
    • 0016612390 scopus 로고
    • Observation of a new EPR transient in chloroplasts that may reflect the electron donor to photosystem II at room temperature
    • Blankenship R.E., Babcock G.T., Warden J.T., Sauer K. Observation of a new EPR transient in chloroplasts that may reflect the electron donor to photosystem II at room temperature. FEBS Lett. 51:1975;287-293.
    • (1975) FEBS Lett. , vol.51 , pp. 287-293
    • Blankenship, R.E.1    Babcock, G.T.2    Warden, J.T.3    Sauer, K.4
  • 5
    • 0017277681 scopus 로고
    • Reaction kinetics for positive charge accumulation on the water side of chloroplast photosystem II
    • Babcock G.T., Blankenship R.E., Sauer K. Reaction kinetics for positive charge accumulation on the water side of chloroplast photosystem II. FEBS Lett. 61:1976;287-293.
    • (1976) FEBS Lett. , vol.61 , pp. 287-293
    • Babcock, G.T.1    Blankenship, R.E.2    Sauer, K.3
  • 6
    • 0035808665 scopus 로고    scopus 로고
    • Amino acid residues that modulate the properties of tyrosine YZ and the manganese cluster in the water oxidizing complex of photosystem II
    • Debus R. Amino acid residues that modulate the properties of tyrosine YZ and the manganese cluster in the water oxidizing complex of photosystem II. Biochim. Biophys. Acta. 1503:2001;164-186.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 164-186
    • Debus, R.1
  • 7
    • 0035808702 scopus 로고    scopus 로고
    • Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation
    • Diner B. Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation. Biochim. Biophys. Acta. 1503:2001;147-163.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 147-163
    • Diner, B.1
  • 8
    • 0023781850 scopus 로고
    • Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system
    • Debus R.J., Barry B.A., Babcock G.T., McIntosh I. Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system. Proc. Natl. Acad. Sci. U. S. A. 85:1988;427-430.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 427-430
    • Debus, R.J.1    Barry, B.A.2    Babcock, G.T.3    McIntosh, I.4
  • 9
    • 0001375803 scopus 로고
    • Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Donor D is a tyrosine residue in the D2 protein
    • Vermaas W.F.J., Rutherford A.W., Hansson Ö. Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: donor D is a tyrosine residue in the D2 protein. Proc. Natl. Acad. Sci. U. S. A. 85:1988;8477-8481.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 8477-8481
    • Vermaas, W.F.J.1    Rutherford, A.W.2    Hansson, Ö.3
  • 10
    • 0024298590 scopus 로고
    • Directed mutagenesis indicates that the donor to P680+ in photosystem II is tyrosine-161 of the D1-polypeptide
    • Debus R.J., Barry B.A., Sithole I., Babcock G.T., McIntosh L. Directed mutagenesis indicates that the donor to P680+ in photosystem II is tyrosine-161 of the D1-polypeptide. Biochemistry. 27:1988;9071-9074.
    • (1988) Biochemistry , vol.27 , pp. 9071-9074
    • Debus, R.J.1    Barry, B.A.2    Sithole, I.3    Babcock, G.T.4    McIntosh, L.5
  • 11
    • 0024976548 scopus 로고
    • Directed alteration of the D1 polypeptide of photosystem II: Evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor P680
    • Metz J.G., Nixon P.J., Rogner M., Brudvig G.W., Diner B.A. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor P680. Biochemistry. 28:1989;6960-6969.
    • (1989) Biochemistry , vol.28 , pp. 6960-6969
    • Metz, J.G.1    Nixon, P.J.2    Rogner, M.3    Brudvig, G.W.4    Diner, B.A.5
  • 12
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • Barry B.A., Babcock G.T. Tyrosine radicals are involved in the photosynthetic oxygen-evolving system. Proc. Natl. Acad. Sci. U. S. A. 84:1987;7099-7103.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 13
    • 0028913561 scopus 로고
    • Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II
    • Koulougliotis D., Tang X.S., Diner B.A., Brudvig G.W. Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II. Biochemistry. 34:1995;2850-2856.
    • (1995) Biochemistry , vol.34 , pp. 2850-2856
    • Koulougliotis, D.1    Tang, X.S.2    Diner, B.A.3    Brudvig, G.W.4
  • 14
    • 0037266023 scopus 로고    scopus 로고
    • Structural analysis of three-spin systems of photosystem II by PELDOR
    • Kawamori A., Katsuta, Hara H. Structural analysis of three-spin systems of photosystem II by PELDOR. Appl. Magn. Reson. 23:2002;557-569.
    • (2002) Appl. Magn. Reson. , vol.23 , pp. 557-569
    • Kawamori, A.1    Katsuta2    Hara, H.3
  • 15
    • 0000180673 scopus 로고
    • An ESEEM study of the oxidized electron donor of plant photosystem II: Evidence that D is an neutral tyrosine radical
    • Evelo R.G., Hoff A.J., Dikanov S.A., Tyryshin A.M. An ESEEM study of the oxidized electron donor of plant photosystem II: evidence that D is an neutral tyrosine radical. Chem. Phys. Lett. 161:1989;479-484.
    • (1989) Chem. Phys. Lett. , vol.161 , pp. 479-484
    • Evelo, R.G.1    Hoff, A.J.2    Dikanov, S.A.3    Tyryshin, A.M.4
  • 16
    • 0000787972 scopus 로고
    • 2H electron spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions
    • 2H electron spin echo envelope modulation (ESEEM) spectroscopic analysis of hydrogen hyperfine interactions. J. Am. Chem. Soc. 116:1994;7332-7340.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7332-7340
    • Warncke, K.1    McCracken, J.2    Babcock, G.T.3
  • 17
    • 0029379730 scopus 로고
    • Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine YZ in photosystem II from multiple-electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution
    • Tommos C., Tang X.-S., Warncke K., Hoganson C.W., Styring S., McCracken J., Diner B.A., Babcock G.T. Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine YZ in photosystem II from multiple-electron magnetic-resonance spectroscopies: implications for photosynthetic oxygen evolution. J. Am. Chem. Soc. 117:1995;10325-10335.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10325-10335
    • Tommos, C.1    Tang, X.-S.2    Warncke, K.3    Hoganson, C.W.4    Styring, S.5    McCracken, J.6    Diner, B.A.7    Babcock, G.T.8
  • 18
    • 0028279040 scopus 로고
    • The dark stable tyrosine radical of photosystem 2 studied in three species using ENDOR and EPR spectroscopies
    • Rigby S.E., Nugent J.H., O'Malley P.J. The dark stable tyrosine radical of photosystem 2 studied in three species using ENDOR and EPR spectroscopies. Biochemistry. 33:1994;1734-1742.
    • (1994) Biochemistry , vol.33 , pp. 1734-1742
    • Rigby, S.E.1    Nugent, J.H.2    O'Malley, P.J.3
  • 20
    • 0025076277 scopus 로고
    • Electron-transfer reactions in manganese-depleted photosystem II
    • Buser C.A., Thompson L.K., Diner B.A., Brudvig G.W. Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry. 29:1990;8977-8985.
    • (1990) Biochemistry , vol.29 , pp. 8977-8985
    • Buser, C.A.1    Thompson, L.K.2    Diner, B.A.3    Brudvig, G.W.4
  • 22
    • 0001105818 scopus 로고
    • Spectral and kinetic pH-dependence of fast and slow signal II in Tris-washed chloroplasts
    • Boussac A., Etienne A.L. Spectral and kinetic pH-dependence of fast and slow signal II in Tris-washed chloroplasts. FEBS Lett. 148:1982;113-116.
    • (1982) FEBS Lett. , vol.148 , pp. 113-116
    • Boussac, A.1    Etienne, A.L.2
  • 23
    • 0034604258 scopus 로고    scopus 로고
    • -radicals in photosystem II determined by high field electron paramagnetic resonance
    • -radicals in photosystem II determined by high field electron paramagnetic resonance. Biochemistry. 39:2000;7826-7834.
    • (2000) Biochemistry , vol.39 , pp. 7826-7834
    • Dorlet, P.1    Rutherford, A.W.2    Un, S.3
  • 24
    • 0028878105 scopus 로고
    • G-Values as a probe of the local protein environment: High-field EPR of tyrosyl radicals in ribonucleotide reductase and photosystem II
    • Un S., Atta M., Fontecave M., Rutherford A.W. g-Values as a probe of the local protein environment: high-field EPR of tyrosyl radicals in ribonucleotide reductase and photosystem II. J. Am. Chem. Soc. 117:1995;10713-10719.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10713-10719
    • Un, S.1    Atta, M.2    Fontecave, M.3    Rutherford, A.W.4
  • 26
    • 0030975546 scopus 로고    scopus 로고
    • The τ-nitrogen of D2 histidine 189 is the hydrogen bond donor to the tyrosine radical YD of photosystem II
    • Campbell K.A., Peloquin J.M., Diner B.A., Tang X.-S., Chisholm D.A., Britt R.D. The τ-nitrogen of D2 histidine 189 is the hydrogen bond donor to the tyrosine radical YD of photosystem II. J. Am. Chem. Soc. 119:1997;4787-4788.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4787-4788
    • Campbell, K.A.1    Peloquin, J.M.2    Diner, B.A.3    Tang, X.-S.4    Chisholm, D.A.5    Britt, R.D.6
  • 27
    • 0032559015 scopus 로고    scopus 로고
    • Hydrogen bonding, solvent exchange, and coupled proton and electron transfer in the oxidation and reduction of redox-active tyrosine Y(Z) in Mn-depleted core complexes of photosystem II
    • Diner B.A., Force D.A., Randall D.W., Britt R.D. Hydrogen bonding, solvent exchange, and coupled proton and electron transfer in the oxidation and reduction of redox-active tyrosine Y(Z) in Mn-depleted core complexes of photosystem II. Biochemistry. 37:1998;17931-17943.
    • (1998) Biochemistry , vol.37 , pp. 17931-17943
    • Diner, B.A.1    Force, D.A.2    Randall, D.W.3    Britt, R.D.4
  • 28
    • 0041806642 scopus 로고    scopus 로고
    • Resolving intermediates in biological proton-coupled electron transfer: A tyrosyl radical prior to proton movement
    • Faller P., Goussias C., Rutherford A.W., Un S. Resolving intermediates in biological proton-coupled electron transfer: a tyrosyl radical prior to proton movement. Proc. Natl. Acad. Sci. U. S. A. 100:2003;8732-8735.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8732-8735
    • Faller, P.1    Goussias, C.2    Rutherford, A.W.3    Un, S.4
  • 30
    • 0001577142 scopus 로고    scopus 로고
    • Structure, dynamics, and energy conversion efficiency in photosystem II
    • D.R. Ort, & C.F. Yocum. Dordrecht: Kluwer Academic Publishing
    • Diner B.A., Babcock G.T. Structure, dynamics, and energy conversion efficiency in photosystem II. Ort D.R., Yocum C.F. Oxygenic Photosynthesis: The Light Reactions. 1996;213-247 Kluwer Academic Publishing, Dordrecht.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 213-247
    • Diner, B.A.1    Babcock, G.T.2
  • 31
    • 0000684952 scopus 로고
    • The oxygen-evolving complex in photosystem II as a metallo-radical enzyme
    • Mathis P. Dordrecht: Kluwer
    • Babcock G.T. The oxygen-evolving complex in photosystem II as a metallo-radical enzyme. Mathis P. Photosynthesis from Light to Shinola. vol. II:1995;209-215 Kluwer, Dordrecht.
    • (1995) Photosynthesis from Light to Shinola , vol.2 , pp. 209-215
    • Babcock, G.T.1
  • 32
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • Hoganson C.W., Babcock G.T. A metalloradical mechanism for the generation of oxygen from water in photosynthesis. Science. 277:1997;1953-1956.
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 33
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • Tommos C., Babcock G.T. Proton and hydrogen currents in photosynthetic water oxidation. Biochim. Biophys. Acta. 1458:2000;199-219.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 34
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II
    • Michel H., Deisenhofer J. Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II. Biochemistry. 27:1988;1-7.
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 35
    • 0022669889 scopus 로고
    • How close is the analogy between PS II and purple bacteria ?
    • Rutherford A.W. How close is the analogy between PS II and purple bacteria ? Biochem. Soc. Trans. 14:1986;15-17.
    • (1986) Biochem. Soc. Trans. , vol.14 , pp. 15-17
    • Rutherford, A.W.1
  • 36
    • 0001967637 scopus 로고
    • How close is the analogy between the reaction centre of PS II and that of purple bacteria? 2. The electron acceptor side
    • Biggins J. Dordrecht: Kluwer
    • Rutherford A.W. How close is the analogy between the reaction centre of PS II and that of purple bacteria? 2. The electron acceptor side. Biggins J. Progress in Photosynthesis Research. vol. 1:1987;277-283 Kluwer, Dordrecht.
    • (1987) Progress in Photosynthesis Research , vol.1 , pp. 277-283
    • Rutherford, A.W.1
  • 38
    • 84990278453 scopus 로고
    • The topology of the plastoquinone and herbicide binding peptides of photosystem II in the thylakoid membrane
    • Trebst A. The topology of the plastoquinone and herbicide binding peptides of photosystem II in the thylakoid membrane. Z. Naturforsch. 41c:1986;240-245.
    • (1986) Z. Naturforsch. , vol.41 , pp. 240-245
    • Trebst, A.1
  • 39
    • 0002799732 scopus 로고    scopus 로고
    • Photosystem II and the quinone-iron-containing reaction centers: Comparisons and evolutionary perspectives
    • H. Baltscheffsky. New York: VCH Publishers
    • Rutherford A.W., Nitschke W. Photosystem II and the quinone-iron- containing reaction centers: comparisons and evolutionary perspectives. Baltscheffsky H. Origin and Evolution of Biological Energy Conversion. 1996;143-175 VCH Publishers, New York.
    • (1996) Origin and Evolution of Biological Energy Conversion , pp. 143-175
    • Rutherford, A.W.1    Nitschke, W.2
  • 41
    • 0020494658 scopus 로고
    • Oxido-reduction kinetics of signal II slow in Tris-washed chloroplasts
    • Boussac A., Etienne A.L. Oxido-reduction kinetics of signal II slow in Tris-washed chloroplasts. Biochem. Biophys. Res. Commun. 109:1982;1200-1205.
    • (1982) Biochem. Biophys. Res. Commun. , vol.109 , pp. 1200-1205
    • Boussac, A.1    Etienne, A.L.2
  • 42
    • 0016698580 scopus 로고
    • The reactivation of EPR signal II in chloroplasts treated with reduced dichlorophenol-indophenol: Evidence against a dark equilibrium between two oxidation states of the oxygen evolving system
    • Velthuys B.R., Visser J.W.M. The reactivation of EPR signal II in chloroplasts treated with reduced dichlorophenol-indophenol: evidence against a dark equilibrium between two oxidation states of the oxygen evolving system. FEBS Lett. 55:1975;109-112.
    • (1975) FEBS Lett. , vol.55 , pp. 109-112
    • Velthuys, B.R.1    Visser, J.W.M.2
  • 43
    • 0026614703 scopus 로고
    • Photoxidation of cytochrome b559 in oxygen-evolving photosystem II
    • Buser C.A., Diner B.A., Brudvig G.W. Photoxidation of cytochrome b559 in oxygen-evolving photosystem II. Biochemistry. 31:1992;11449-11459.
    • (1992) Biochemistry , vol.31 , pp. 11449-11459
    • Buser, C.A.1    Diner, B.A.2    Brudvig, G.W.3
  • 44
    • 0030448542 scopus 로고    scopus 로고
    • A model for the photosystem II reaction center core including the structure of the primary donor P680
    • Svensson B., Etchebest C., Tuffery P., van Kan P., Smith J., Styring S. A model for the photosystem II reaction center core including the structure of the primary donor P680. Biochemistry. 35:1996;14486-14502.
    • (1996) Biochemistry , vol.35 , pp. 14486-14502
    • Svensson, B.1    Etchebest, C.2    Tuffery, P.3    Van Kan, P.4    Smith, J.5    Styring, S.6
  • 45
    • 34249842840 scopus 로고
    • A three dimensional model of the photosystem II reaction centre of Pisum sativum
    • Ruffle S.V., Donnelly D., Blundell T.L., Nugent J.H.A. A three dimensional model of the photosystem II reaction centre of Pisum sativum. Photosynth. Res. 34:1992;287-300.
    • (1992) Photosynth. Res. , vol.34 , pp. 287-300
    • Ruffle, S.V.1    Donnelly, D.2    Blundell, T.L.3    Nugent, J.H.A.4
  • 46
    • 0027286757 scopus 로고
    • Modified EPR spectra of the tyrosineD radical in photosystem II in site-directed mutants of Synechocystis sp. PCC 6803: Identification of side chains in the immediate vicinity of tyrosineD on the D2 protein
    • Tommos C., Davidsson L., Svensson B., Madsen C., Vermaas W., Styring S. Modified EPR spectra of the tyrosineD radical in photosystem II in site-directed mutants of Synechocystis sp. PCC 6803: identification of side chains in the immediate vicinity of tyrosineD on the D2 protein. Biochemistry. 32:1993;5436-5441.
    • (1993) Biochemistry , vol.32 , pp. 5436-5441
    • Tommos, C.1    Davidsson, L.2    Svensson, B.3    Madsen, C.4    Vermaas, W.5    Styring, S.6
  • 47
    • 0037195309 scopus 로고    scopus 로고
    • Biogenesis, assembly and turnover of photosystem II units
    • Baena-Gonzalez E., Aro E.M. Biogenesis, assembly and turnover of photosystem II units. Philos. Trans. R. Soc., B. 357:2002;1451-1459.
    • (2002) Philos. Trans. R. Soc., B , vol.357 , pp. 1451-1459
    • Baena-Gonzalez, E.1    Aro, E.M.2
  • 48
    • 0032483036 scopus 로고    scopus 로고
    • Coupled activation of donor and the acceptor side of photosystem II during photoactivation of the oxygen evolving cluster
    • Rova M., Mamedov F., Magnuson A., Fredriksson P.-O., Styring S. Coupled activation of donor and the acceptor side of photosystem II during photoactivation of the oxygen evolving cluster. Biochemistry. 37:1998;11039-11045.
    • (1998) Biochemistry , vol.37 , pp. 11039-11045
    • Rova, M.1    Mamedov, F.2    Magnuson, A.3    Fredriksson, P.-O.4    Styring, S.5
  • 49
    • 0037154125 scopus 로고    scopus 로고
    • A functional role for tyrosine D in assembly of the inorganic core of the water oxidase complex of photosystem II and the kinetics of water oxidation
    • Ananyev G.M., Sakiyan I., Diner B.A., Dismukes G.C. A functional role for tyrosine D in assembly of the inorganic core of the water oxidase complex of photosystem II and the kinetics of water oxidation. Biochemistry. 41:2002;974-980.
    • (2002) Biochemistry , vol.41 , pp. 974-980
    • Ananyev, G.M.1    Sakiyan, I.2    Diner, B.A.3    Dismukes, G.C.4
  • 50
    • 0014400748 scopus 로고
    • Analysis of the interactions between the two photosystems in isolated chloroplasts
    • Joliot P., Joliot A., Kok B. 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    Kok, B.3
  • 51
    • 0000119587 scopus 로고
    • The reduction of the oxygen-evolving system in chloroplasts by thylakoid components
    • Vermaas W.F.J., Renger G., Dohnt G. The reduction of the oxygen-evolving system in chloroplasts by thylakoid components. Biochim. Biophys. Acta. 764:1984;194-202.
    • (1984) Biochim. Biophys. Acta , vol.764 , pp. 194-202
    • Vermaas, W.F.J.1    Renger, G.2    Dohnt, G.3
  • 52
    • 1842290620 scopus 로고
    • 2 evolving enzyme of Photosystem II - Recent developments
    • 2 evolving enzyme of Photosystem II - recent developments. Physiol. Vég. 23:1985;425-434.
    • (1985) Physiol. Vég. , vol.23 , pp. 425-434
    • Zimmerman, J.L.1    Rutherford, A.W.2
  • 53
    • 33749844070 scopus 로고
    • In the oxygen evolving complex of photosystem II the S0 state is oxidised to the S1 state by D+ (Signal II slow)
    • Styring S., Rutherford A.W. In the oxygen evolving complex of photosystem II the S0 state is oxidised to the S1 state by D+ (Signal II slow). Biochemistry. 26:1987;2401-2405.
    • (1987) Biochemistry , vol.26 , pp. 2401-2405
    • Styring, S.1    Rutherford, A.W.2
  • 54
    • 0027384113 scopus 로고
    • Generation, oxidation by the oxidized form of the tyrosine of polypeptide D2, and possible electronic configuration of the redox states S-0, S-1, and S-2 of the water oxidase in isolated spinach thylakoids
    • Messinger J., Renger G. Generation, oxidation by the oxidized form of the tyrosine of polypeptide D2, and possible electronic configuration of the redox states S-0, S-1, and S-2 of the water oxidase in isolated spinach thylakoids. Biochemistry. 32:1993;9379-9386.
    • (1993) Biochemistry , vol.32 , pp. 9379-9386
    • Messinger, J.1    Renger, G.2
  • 55
    • 48549111809 scopus 로고
    • Midpoint potential of signal II (slow) in Tris-washed photosystem II particles
    • Boussac A., Etienne A.L. Midpoint potential of signal II (slow) in Tris-washed photosystem II particles. Biochim. Biophys. Acta. 766:1984;576-581.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 576-581
    • Boussac, A.1    Etienne, A.L.2
  • 56
    • 0026096798 scopus 로고
    • PH dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials
    • Vass I., Styring S. pH dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials. Biochemistry. 30:1991;830-839.
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 57
    • 0028180062 scopus 로고
    • The origin of 40-50°thermoluminescence bands in photosystem II
    • Johnson G., Boussac A., Rutherford A.W. The origin of 40-50°thermoluminescence bands in photosystem II. Biochim. Biophys. Acta. 1184:1994;85-92.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 85-92
    • Johnson, G.1    Boussac, A.2    Rutherford, A.W.3
  • 58
    • 0000615085 scopus 로고
    • EPR study of charge equilibrium at low temperatures in the S2 state of oxygen-evolving photosystem II particles
    • Kawamori A., Satoh J., Inui T., Satoh K. EPR study of charge equilibrium at low temperatures in the S2 state of oxygen-evolving photosystem II particles. FEBS Lett. 217:1987;34-43.
    • (1987) FEBS Lett. , vol.217 , pp. 34-43
    • Kawamori, A.1    Satoh, J.2    Inui, T.3    Satoh, K.4
  • 60
    • 0029856747 scopus 로고    scopus 로고
    • Fourier transform infrared difference study of tyrosineD oxidation and plastoquinone QA reduction in photosystem II
    • Hienerwadel R., Boussac A., Breton J., Berthomieu C. Fourier transform infrared difference study of tyrosineD oxidation and plastoquinone QA reduction in photosystem II. Biochemistry. 35:1996;15447-15460.
    • (1996) Biochemistry , vol.35 , pp. 15447-15460
    • Hienerwadel, R.1    Boussac, A.2    Breton, J.3    Berthomieu, C.4
  • 61
    • 0037207119 scopus 로고    scopus 로고
    • Replacement of tyrosine D with phenylalanine affects the normal proton transfer pathways for the reduction of P680(+) in oxygen-evolving Photosystem II particles from Chlamydomonas
    • Jeans C., Schilstra M.J., Ray N., Husain S., Minagawa J., Nugent J.H.A., Klug D.R. Replacement of tyrosine D with phenylalanine affects the normal proton transfer pathways for the reduction of P680(+) in oxygen-evolving Photosystem II particles from Chlamydomonas. Biochemistry. 41:2002;15754-15761.
    • (2002) Biochemistry , vol.41 , pp. 15754-15761
    • Jeans, C.1    Schilstra, M.J.2    Ray, N.3    Husain, S.4    Minagawa, J.5    Nugent, J.H.A.6    Klug, D.R.7
  • 62
    • 0027526897 scopus 로고
    • Removal of stable tyrosine radical D+ affects the structure or redox properties of tyrosine Z in manganese-depleted photosystem II particles from Synechocystis 6803
    • Boerner R.J., Bixby K.A., Nguyen A.P., Noren G.H., Debus R.J., Barry B.A. Removal of stable tyrosine radical D+ affects the structure or redox properties of tyrosine Z in manganese-depleted photosystem II particles from Synechocystis 6803. J. Biol. Chem. 268:1993;1817-1823.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1817-1823
    • Boerner, R.J.1    Bixby, K.A.2    Nguyen, A.P.3    Noren, G.H.4    Debus, R.J.5    Barry, B.A.6
  • 64
    • 0035822664 scopus 로고    scopus 로고
    • Site-directed mutations at D1-His198 and D2-His197 of Photosystem II in Synechocystis PCC 6803: Sites of primary charge separation and cation and triplet stabilization
    • Diner B.A., Schlodder E., Nixon P.J., Coleman W.J., Rappaport F., Lavergne J., Vermaas W.F.J., Chisholm D.A. Site-directed mutations at D1-His198 and D2-His197 of Photosystem II in Synechocystis PCC 6803: Sites of primary charge separation and cation and triplet stabilization. Biochemistry. 40:2001;9265-9281.
    • (2001) Biochemistry , vol.40 , pp. 9265-9281
    • Diner, B.A.1    Schlodder, E.2    Nixon, P.J.3    Coleman, W.J.4    Rappaport, F.5    Lavergne, J.6    Vermaas, W.F.J.7    Chisholm, D.A.8
  • 65
    • 0036999722 scopus 로고    scopus 로고
    • Structure dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis
    • Diner B.A., Rappaport F. Structure dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis. Annu. Rev. Plant Biol. 53:2002;551-580.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 66
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution. Nature. 409:2001;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
  • 67
    • 0025891869 scopus 로고
    • A chlorophyll tilted 30°relative to the membrane in the photosystem II reaction centre
    • van Mieghem F.J.E., Satoh K., Rutherford A.W. A chlorophyll tilted 30°relative to the membrane in the photosystem II reaction centre. Biochim. Biophys. Acta. 1058:1991;379-385.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 379-385
    • Van Mieghem, F.J.E.1    Satoh, K.2    Rutherford, A.W.3
  • 68
    • 0000087299 scopus 로고
    • Spectral properties of stabilised D1/D2cytochrome b559 photosystem II reaction centre complex
    • Tetenkin V.L., Gulyaev B.A., Seibert M., Rubin A.B. Spectral properties of stabilised D1/D2cytochrome b559 photosystem II reaction centre complex. FEBS Lett. 250:1989;459-463.
    • (1989) FEBS Lett. , vol.250 , pp. 459-463
    • Tetenkin, V.L.1    Gulyaev, B.A.2    Seibert, M.3    Rubin, A.B.4
  • 69
    • 0025183698 scopus 로고
    • D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligoffhhiza: Correlation between complex integrity, spectroscopic properties, photochemical activity and pigment composition
    • Braun P., Greenberg B.M., Scherz A. D1-D2-cytochrome b559 complex from the aquatic plant Spirodela oligoffhhiza: correlation between complex integrity, spectroscopic properties, photochemical activity and pigment composition. Biochemistry. 29:1990;10376-10387.
    • (1990) Biochemistry , vol.29 , pp. 10376-10387
    • Braun, P.1    Greenberg, B.M.2    Scherz, A.3
  • 70
    • 0028960993 scopus 로고
    • Charge recombination reactions in photosystem II: 2. Transient absorbance difference spectra and their temperature dependence
    • Hillmann B., Brettel K., van Mieghem F., Kamlowski A., Rutherford A.W., Schlodder E. Charge recombination reactions in photosystem II: 2. Transient absorbance difference spectra and their temperature dependence. Biochemistry. 34:1995;4814-4827.
    • (1995) Biochemistry , vol.34 , pp. 4814-4827
    • Hillmann, B.1    Brettel, K.2    Van Mieghem, F.3    Kamlowski, A.4    Rutherford, A.W.5    Schlodder, E.6
  • 71
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes
    • Berthold D.A., Babcock G.T., Yocum C.F. A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes. FEBS Lett. 134:1981;231-234.
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 72
    • 0021755973 scopus 로고
    • X ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer J., Epp O., Miki K., Huber R., Michel H. X ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180:1984;385-398.
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 73
    • 1942506305 scopus 로고
    • Light energy transduction in photosynthesis higher plants and bacterial models
    • S.E. Stevens, & D.A. Bryant. Rockville, Maryland: American Society of Plant Physiologists
    • Rutherford A.W. Light energy transduction in photosynthesis higher plants and bacterial models. Stevens S.E., Bryant D.A. Photosystem II, The Oxygen Evolving Photosystem. 1988;163-177 American Society of Plant Physiologists, Rockville, Maryland.
    • (1988) Photosystem II, the Oxygen Evolving Photosystem , pp. 163-177
    • Rutherford, A.W.1
  • 74
    • 0024678988 scopus 로고
    • Photosystem II: The water splitting enzyme
    • Rutherford A.W. Photosystem II: the water splitting enzyme. Trends in Biochem. Sci. 14:1989;227-232.
    • (1989) Trends in Biochem. Sci. , vol.14 , pp. 227-232
    • Rutherford, A.W.1


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