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Volumn 43, Issue 21, 2004, Pages 6783-6792

Hydroxyl radical generation by photosystem II

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; COLORIMETRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; PARAMAGNETIC RESONANCE; PHOTOCHEMICAL REACTIONS; REACTION KINETICS;

EID: 2542632099     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036219i     Document Type: Article
Times cited : (112)

References (78)
  • 1
    • 0030007698 scopus 로고    scopus 로고
    • Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II
    • Nugent, J. H. A. (1996) Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II, Eur. J. Biochem. 237, 519-531.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 519-531
    • Nugent, J.H.A.1
  • 2
    • 0000561603 scopus 로고    scopus 로고
    • Oxygen evolution
    • (Ort, D., Yocum, C., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Britt, R. D. (1996) Oxygen Evolution, in Oxygenic Photosynthesis: The Light Reactions (Ort, D., Yocum, C., Eds.) pp 137-164, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 137-164
    • Britt, R.D.1
  • 3
    • 0001577142 scopus 로고    scopus 로고
    • Structure, dynamics, and energy conversion efficiency in photosystem II
    • (Ort, D., Yocum, C., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Diner, B. A., and Babcock, G. T. (1996) Structure, Dynamics, and Energy Conversion Efficiency in Photosystem II, in Oxygenic Photosynthesis: The Light Reactions (Ort, D., Yocum, C., Eds.) pp 213-247, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 213-247
    • Diner, B.A.1    Babcock, G.T.2
  • 4
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis
    • Diner, B. A., and Rappaport, F. (2002) Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis, Annu. Rev. Plant. Biol. 53, 551-580.
    • (2002) Annu. Rev. Plant. Biol. , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 6
    • 0002305863 scopus 로고    scopus 로고
    • Oxygen metabolism and electron transport in photosynthesis
    • (Scandalios, J. G., Ed.), Cold Spring Harbor Laboratory Press, Plainview, NY
    • Foyer, C. (1997) Oxygen Metabolism and Electron Transport in Photosynthesis, in Oxidative Stress and the Molecular Biology of Antioxidant Defences (Scandalios, J. G., Ed.) pp 587-621, Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1997) Oxidative Stress and the Molecular Biology of Antioxidant Defences , pp. 587-621
    • Foyer, C.1
  • 7
    • 0002174971 scopus 로고
    • Oxygen activation and oxygen toxicity
    • Elstner, E. F. (1982) Oxygen activation and oxygen toxicity, Annu. Rev. Plant. Physiol. 33, 73-96.
    • (1982) Annu. Rev. Plant. Physiol. , vol.33 , pp. 73-96
    • Elstner, E.F.1
  • 9
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada, K. (1999) The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons, Annu. Rev. Plant. Physiol. Plant. Mol. Biol. 50, 601-639.
    • (1999) Annu. Rev. Plant. Physiol. Plant. Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 11
    • 0032879783 scopus 로고    scopus 로고
    • Voltammetric detection of superoxide production by photosystem II
    • Cleland, R. E., and Grace, S. C. (1999) Voltammetric detection of superoxide production by photosystem II, FEBS Lett. 457, 348-352.
    • (1999) FEBS Lett. , vol.457 , pp. 348-352
    • Cleland, R.E.1    Grace, S.C.2
  • 12
    • 0033381416 scopus 로고    scopus 로고
    • Superoxide and hydroxyl radical generation, and superoxide dismutase in PSII membrane fragments from wheat
    • Navari-Izzo, F., Pinzino, C., Quartacci, M. F., and Sgherri, C. L. M. (1999) Superoxide and hydroxyl radical generation, and superoxide dismutase in PSII membrane fragments from wheat, Free Radical Res. 30, 3-9.
    • (1999) Free Radical Res. , vol.30 , pp. 3-9
    • Navari-Izzo, F.1    Pinzino, C.2    Quartacci, M.F.3    Sgherri, C.L.M.4
  • 13
    • 0037232722 scopus 로고    scopus 로고
    • Study on the photogeneration of superoxide radicals in Photosystem II with EPR spin trapping techniques
    • Zhang, S., Weng, J., Pan, J., Tu, T., Yao, S., and Xu, C. (2003) Study on the photogeneration of superoxide radicals in Photosystem II with EPR spin trapping techniques, Photosynth. Res. 75, 41-48.
    • (2003) Photosynth. Res. , vol.75 , pp. 41-48
    • Zhang, S.1    Weng, J.2    Pan, J.3    Tu, T.4    Yao, S.5    Xu, C.6
  • 14
    • 0028938833 scopus 로고
    • Superoxide contributes to the rapid inactivation of specific secondary donors of the photosystem II reaction center during photodamage of manganese-depleted photosystem II membranes
    • Chen, G. X., Blubaugh, D. J., Homann, P. H., Golbeck, J. G., and Cheniae, G. M. (1995) Superoxide contributes to the rapid inactivation of specific secondary donors of the photosystem II reaction center during photodamage of manganese-depleted photosystem II membranes, Biochemistry 34, 2317-2332.
    • (1995) Biochemistry , vol.34 , pp. 2317-2332
    • Chen, G.X.1    Blubaugh, D.J.2    Homann, P.H.3    Golbeck, J.G.4    Cheniae, G.M.5
  • 15
    • 0026496536 scopus 로고
    • Photoinhibition of hydroxylamine-extracted photosystem II membranes: Studies of the mechanism
    • Chen, G. X., Kazimir, J., and Cheniae, G. M. (1992) Photoinhibition of hydroxylamine-extracted photosystem II membranes: studies of the mechanism, Biochemistry 31, 11072-11083.
    • (1992) Biochemistry , vol.31 , pp. 11072-11083
    • Chen, G.X.1    Kazimir, J.2    Cheniae, G.M.3
  • 16
    • 0001477239 scopus 로고
    • 2 accessibility to the Photosystem II donor side in protein-depleted inside-out thylakoids measured as flash-induced oxygen production
    • 2 accessibility to the Photosystem II donor side in protein-depleted inside-out thylakoids measured as flash-induced oxygen production, Biochim. Biophys. Acta 848, 359-363.
    • (1986) Biochim. Biophys. Acta , vol.848 , pp. 359-363
    • Schröder, W.P.1    Åkerlund, H.-E.2
  • 17
    • 0001640810 scopus 로고
    • Photoproduction of hydrogen peroxide in photosystem II membrane fragments: A comparison of four signals
    • Klimov, V., Ananyev, G., Zastryzhnava, O., Wydrzynski, T., and Renger, G. (1993) Photoproduction of hydrogen peroxide in photosystem II membrane fragments: a comparison of four signals, Photosynth. Res. 38, 409-416.
    • (1993) Photosynth. Res. , vol.38 , pp. 409-416
    • Klimov, V.1    Ananyev, G.2    Zastryzhnava, O.3    Wydrzynski, T.4    Renger, G.5
  • 19
    • 0026743378 scopus 로고
    • The oxygen-evolving complex requires chloride to prevent hydrogen peroxide formation
    • Fine, P. L., and Frasch, W. D. (1992) The oxygen-evolving complex requires chloride to prevent hydrogen peroxide formation, Biochemistry 31, 12204-12210.
    • (1992) Biochemistry , vol.31 , pp. 12204-12210
    • Fine, P.L.1    Frasch, W.D.2
  • 20
    • 2542541802 scopus 로고    scopus 로고
    • 2 Produced by Photosystem II in Photoinhibition
    • (Garab, G., Ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 2 Produced by Photosystem II in Photoinhibition, in Photosynthesis: Mechanisms and Effects (Garab, G., Ed.) Vol. 3, pp 2135-2138, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1998) Photosynthesis: Mechanisms and Effects , vol.3 , pp. 2135-2138
    • Krieger, A.1    Rutherford, A.W.2
  • 21
    • 1042290468 scopus 로고    scopus 로고
    • Production of reactive oxygen species in chloride- and calcium depleted photosystem II and their involvement in photoinhibition
    • Arató, A., Bondarava, N., and Krieger-Liszkay, A. (2004) Production of reactive oxygen species in chloride- and calcium depleted photosystem II and their involvement in photoinhibition, Biochim. Biophys. Acta 1608, 171-180.
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 171-180
    • Arató, A.1    Bondarava, N.2    Krieger-Liszkay, A.3
  • 22
    • 0000173387 scopus 로고
    • Hydrogen peroxide production in photosystem II preparations
    • (Baltscheffsky, M., Ed.), Kluwer Academic Publisher, Dordrecht, The Netherlands
    • Schröder, W. P., and Åkerlund, H.-E. (1990) Hydrogen Peroxide Production in Photosystem II Preparations, in Current Research in Photosynthesis (Baltscheffsky, M., Ed.) Vol. 1, pp 901-904, Kluwer Academic Publisher, Dordrecht, The Netherlands.
    • (1990) Current Research in Photosynthesis , vol.1 , pp. 901-904
    • Schröder, W.P.1    Åkerlund, H.-E.2
  • 24
    • 0035795165 scopus 로고    scopus 로고
    • Photoreducible high spin iron electron paramagnetic resonance signals in dark-adapted Photosystem II: Are they oxidised nonhaem iron formed from interaction of oxygen with PSII electron acceptors?
    • Nugent, J. H. A. (2001) Photoreducible high spin iron electron paramagnetic resonance signals in dark-adapted Photosystem II: are they oxidised nonhaem iron formed from interaction of oxygen with PSII electron acceptors? Biochim. Biophys. Acta 1504, 288-298.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 288-298
    • Nugent, J.H.A.1
  • 25
    • 0006976349 scopus 로고
    • 2 evolution from the apparent S-state transitions in Photosystem II by lauroylcholine chloride: Possible implicationsin the photosynthetic water-splitting mechanism
    • 2 evolution from the apparent S-state transitions in Photosystem II by lauroylcholine chloride: possible implicationsin the photosynthetic water-splitting mechanism, Biochim. Biophys. Acta 809, 125-136.
    • (1985) Biochim. Biophys. Acta , vol.809 , pp. 125-136
    • Wydrzynski, T.1    Huggins, B.J.2    Jursinic, P.A.3
  • 26
    • 0030042115 scopus 로고    scopus 로고
    • On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism
    • Wydrzynski, T., Hillier, W., and Messinger, J. (1996) On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism, Physiol. Plant. 96, 342-350.
    • (1996) Physiol. Plant. , vol.96 , pp. 342-350
    • Wydrzynski, T.1    Hillier, W.2    Messinger, J.3
  • 27
    • 0029914038 scopus 로고    scopus 로고
    • Photoinhibition of photosystem II from higher plants. Effect of copper inhibition
    • Yruela, I., Pueyo, J. J., Alonso, P. J., and Picorel, R. (1996) Photoinhibition of photosystem II from higher plants. Effect of copper inhibition, J. Biol. Chem. 271(44), 27408-27415.
    • (1996) J. Biol. Chem. , vol.271 , Issue.44 , pp. 27408-27415
    • Yruela, I.1    Pueyo, J.J.2    Alonso, P.J.3    Picorel, R.4
  • 28
    • 0032515935 scopus 로고    scopus 로고
    • 2-evolving complex does not dismutate hydrogen peroxide
    • 2-evolving complex does not dismutate hydrogen peroxide, Biochemistry 37, 5052-5059.
    • (1998) Biochemistry , vol.37 , pp. 5052-5059
    • Sheptovitsky, Y.G.1    Brudvig, G.W.2
  • 29
    • 18744409047 scopus 로고    scopus 로고
    • Singlet oxygen production in herbicide-treated photosystem II
    • Fufezan, C., Rutherford, A. W., and Krieger-Liszkay, A. (2002) Singlet oxygen production in herbicide-treated photosystem II, FEBS Lett. 532, 407-410.
    • (2002) FEBS Lett. , vol.532 , pp. 407-410
    • Fufezan, C.1    Rutherford, A.W.2    Krieger-Liszkay, A.3
  • 30
    • 0028131199 scopus 로고
    • Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy
    • Hideg, E., Spetea, C., and Vass, I. (1994) Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy, Biochim. Biophys. Acta 1186, 143-152.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 143-152
    • Hideg, E.1    Spetea, C.2    Vass, I.3
  • 31
    • 0037015995 scopus 로고    scopus 로고
    • Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses
    • Zolla, L., and Rinalducci, S. (2002) Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses, Biochemistry 41, 14391-14402.
    • (2002) Biochemistry , vol.41 , pp. 14391-14402
    • Zolla, L.1    Rinalducci, S.2
  • 32
    • 0032619789 scopus 로고    scopus 로고
    • The mechanism of "Fenton-Like" reactions and their importance for biological systems. A biologist's view
    • (Sigel, A., Sigel, H., Eds.), Marcel Dekker, Inc, New York
    • Liochev, S. I. (1999) The Mechanism of "Fenton-Like" Reactions and Their Importance for Biological Systems. A Biologist's View, in Metals in Biological Systems (Sigel, A., Sigel, H., Eds.) Vol. 36, pp 1-39, Marcel Dekker, Inc, New York.
    • (1999) Metals in Biological Systems , vol.36 , pp. 1-39
    • Liochev, S.I.1
  • 33
    • 0032605403 scopus 로고    scopus 로고
    • Free radicals as a results of dioxygen metabolism
    • (Sigel, A., Sigel, H., Eds.), Marcel Dekker, Inc, New York
    • Branchaud, B. P. (1999) Free Radicals as a Results of Dioxygen Metabolism, in Metals in Biological Systems (Sigel, A., Sigel, H., Eds.) Vol. 36, pp 79-102, Marcel Dekker, Inc, New York.
    • (1999) Metals in Biological Systems , vol.36 , pp. 79-102
    • Branchaud, B.P.1
  • 34
    • 0008058711 scopus 로고
    • Reactive oxygen species: Electron donor-hydrogen peroxide complex instead of free radicals?
    • Elstner, E. F., Osswald, W., and Konze, J. R. (1980) Reactive oxygen species: electron donor-hydrogen peroxide complex instead of free radicals? FEBS Lett. 121, 219-221.
    • (1980) FEBS Lett. , vol.121 , pp. 219-221
    • Elstner, E.F.1    Osswald, W.2    Konze, J.R.3
  • 35
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E. R. (1993) Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions, Annu. Rev. Biochem. 62, 797-821.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 37
    • 2542609348 scopus 로고    scopus 로고
    • x; M = Fe, Cu, Co, Mn]/hydroperoxide-induced activation of dioxygen for the oxygenation of hydrocarbons: Oxygenated Fenton chemistry
    • x; M = Fe, Cu, Co, Mn]/hydroperoxide-induced activation of dioxygen for the oxygenation of hydrocarbons: oxygenated Fenton chemistry, Acc. Chem. Res. 29, 409-416.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 409-416
    • Sawyer, D.T.1    Sobkowiak, A.2    Matsushita, T.3
  • 38
    • 0032053161 scopus 로고    scopus 로고
    • Oxygen toxicity: A radical explanation
    • Fridovich, I. (1998) Oxygen toxicity: a radical explanation, J. Exp. Biol. 201, 1203-1209.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1203-1209
    • Fridovich, I.1
  • 40
    • 0001080723 scopus 로고    scopus 로고
    • Nature of activated bleomycin
    • Burger, R. M. (2000) Nature of activated bleomycin, Struct. Bonding 97, 287-303.
    • (2000) Struct. Bonding , vol.97 , pp. 287-303
    • Burger, R.M.1
  • 41
    • 0542422859 scopus 로고    scopus 로고
    • Heme oxygenase mechanism: Evidences for an electrophilic, ferric peroxide species
    • Ortiz de Montellano, P. R. (1998) Heme oxygenase mechanism: evidences for an electrophilic, ferric peroxide species, Acc. Chem. Res. 31, 543-549.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 543-549
    • Ortiz De Montellano, P.R.1
  • 42
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, F. E., Jr., Verhagen, M. F. J. M., Cui, X., and Adams, M. W. W. (1999) Anaerobic microbes: oxygen detoxification without superoxide dismutase, Science 286, 306-309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney Jr., F.E.1    Verhagen, M.F.J.M.2    Cui, X.3    Adams, M.W.W.4
  • 43
    • 0034703748 scopus 로고    scopus 로고
    • Superoxide reactivity of rubredoxin oxidoreductase (desulfoferrodoxin) from Desulfovibrio vulgaris: A pulse radiolysis study
    • Coulter, E. D., Emerson, J. P., Kurtz, D. M., Jr., and Cabelli, D. E. (2000) Superoxide reactivity of rubredoxin oxidoreductase (desulfoferrodoxin) from Desulfovibrio vulgaris: a pulse radiolysis study, J. Am. Chem. Soc. 122, 11555-11556.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11555-11556
    • Coulter, E.D.1    Emerson, J.P.2    Kurtz Jr., D.M.3    Cabelli, D.E.4
  • 44
    • 0037042234 scopus 로고    scopus 로고
    • Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii
    • Mathé, C., Mattioli, T. A., Horner, O., Lombard, M., Latour, J.-M., Fontecave, M., and Nivière, V. (2002) Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii, J. Am. Chem. Soc. 124, 4966-4967.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4966-4967
    • Mathé, C.1    Mattioli, T.A.2    Horner, O.3    Lombard, M.4    Latour, J.-M.5    Fontecave, M.6    Nivière, V.7
  • 45
    • 0000075484 scopus 로고
    • A highly resolved, oxygen evolving photosystem II preparation from spinach thylakoid membranes
    • Berthold, D. A., Babcock, G. T., and Yocum, C. F. (1980) A highly resolved, oxygen evolving photosystem II preparation from spinach thylakoid membranes, FEBS Lett. 134, 231-234.
    • (1980) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 46
    • 0001625998 scopus 로고
    • Isolation of a photosystem 2 preparation from higher plants with highly enriched oxygen evolution activity
    • Ford, R. C., and Evans, M. C. W. (1983) Isolation of a photosystem 2 preparation from higher plants with highly enriched oxygen evolution activity, FEBS Lett. 160, 159-164.
    • (1983) FEBS Lett. , vol.160 , pp. 159-164
    • Ford, R.C.1    Evans, M.C.W.2
  • 47
    • 48549108839 scopus 로고
    • A new EPR signal attributed to the primary plastoquinone acceptor in Photosystem II
    • Rutherford, A. W., and Zimmermann, J. L. (1984) A new EPR signal attributed to the primary plastoquinone acceptor in Photosystem II, Biochim. Biophys. Acta 767, 168-175.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 168-175
    • Rutherford, A.W.1    Zimmermann, J.L.2
  • 48
    • 0000865063 scopus 로고
    • EPR measurements on the effect of bicarbonate and triazine resistance in the acceptor side of Photosystem II
    • Vermass, W. F. J., and Rutherford, A. W. (1984) EPR measurements on the effect of bicarbonate and triazine resistance in the acceptor side of Photosystem II, FEBS Lett. 175, 243-248.
    • (1984) FEBS Lett. , vol.175 , pp. 243-248
    • Vermass, W.F.J.1    Rutherford, A.W.2
  • 49
    • 0001700716 scopus 로고
    • 400, a high-potential electron acceptor of Photosystem II, with the iron of the quinone-iron complex
    • 400, a high-potential electron acceptor of Photosystem II, with the iron of the quinone-iron complex, Biochim. Biophys. Acta 849, 264-275.
    • (1986) Biochim. Biophys. Acta , vol.849 , pp. 264-275
    • Petrouleas, V.1    Diner, B.A.2
  • 50
    • 0026530490 scopus 로고
    • Stabilities of hydroxyl radical spin adducts of PBN-type spin traps
    • Janzen, E. G., Kotake, Y., and Hinton, R. D. (1992) Stabilities of hydroxyl radical spin adducts of PBN-type spin traps, Free Radical Biol. Med. 12, 169-173.
    • (1992) Free Radical Biol. Med. , vol.12 , pp. 169-173
    • Janzen, E.G.1    Kotake, Y.2    Hinton, R.D.3
  • 51
    • 0027957717 scopus 로고
    • A kinetic approach to the selection of a sensitive spin trapping system for the detection of hydroxyl radical
    • Pou, S., Ramos, C. L., Gladwell, T., Renks, E., Centra, M., Young, D., Cohen, M. S., and Rosen, G. M. (1994) A kinetic approach to the selection of a sensitive spin trapping system for the detection of hydroxyl radical, Anal. Biochem. 217, 76-83.
    • (1994) Anal. Biochem. , vol.217 , pp. 76-83
    • Pou, S.1    Ramos, C.L.2    Gladwell, T.3    Renks, E.4    Centra, M.5    Young, D.6    Cohen, M.S.7    Rosen, G.M.8
  • 52
    • 0033965592 scopus 로고    scopus 로고
    • 2-ethoxycarbonyl-2-methyl-3,4-dihydro-2H-pyrrole-1-oxide: Evaluation of the spin trapping properties
    • Olive, G., Mercier, A., Moigne, F. L., Rockenbauer, A., Tordo, P. (2000) 2-ethoxycarbonyl-2-methyl-3,4-dihydro-2H-pyrrole-1-oxide: evaluation of the spin trapping properties, Free Radical Biol. Med. 28, 403-408.
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 403-408
    • Olive, G.1    Mercier, A.2    Moigne, F.L.3    Rockenbauer, A.4    Tordo, P.5
  • 54
    • 0026011829 scopus 로고
    • Protection of reaction center II from photodamage by low temperature and anaerobiosis in spinach chloroplasts
    • Kirilovsky, D., and Etienne, A.-L. (1991) Protection of reaction center II from photodamage by low temperature and anaerobiosis in spinach chloroplasts, FEBS Lett. 279, 201-204.
    • (1991) FEBS Lett. , vol.279 , pp. 201-204
    • Kirilovsky, D.1    Etienne, A.-L.2
  • 55
    • 0019847142 scopus 로고
    • Stoichiometry, inhibitor sensitivity, and organization of manganese associated with photosynthetic oxygen evolution
    • Yocum, C. F., Yerkes, C. T., Blankenship, R. E., Sharp, R. R., and Babcock, G. T. (1981) Stoichiometry, inhibitor sensitivity, and organization of manganese associated with photosynthetic oxygen evolution, Proc. Natl. Acad. Sci. U.S.A. 78, 7507-7511.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 7507-7511
    • Yocum, C.F.1    Yerkes, C.T.2    Blankenship, R.E.3    Sharp, R.R.4    Babcock, G.T.5
  • 56
    • 0040356813 scopus 로고
    • Hydrogen peroxide oxidation catalyzed by chloride-depleted thylakoid membranes
    • Sandusky, P. O., and Yocum, C. F. (1988) Hydrogen peroxide oxidation catalyzed by chloride-depleted thylakoid membranes, Biochim. Biophys. Acta 936, 149-156.
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 149-156
    • Sandusky, P.O.1    Yocum, C.F.2
  • 57
    • 45949113263 scopus 로고
    • B binding site. I. Quinones, kinetics and pH-dependence
    • B binding site. I. Quinones, kinetics and pH-dependence, Biochim. Biophys. Acta 893, 126-137.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 126-137
    • Petrouleas, V.1    Diner, B.A.2
  • 60
    • 0026491065 scopus 로고
    • Photoinhibition affects the non-heme iron center in photosystem II
    • Gleiter, H. M., Nugent, J. H. A., Haag, E., and Renger, G. (1992) Photoinhibition affects the non-heme iron center in photosystem II, FEBS Lett. 313, 75-79.
    • (1992) FEBS Lett. , vol.313 , pp. 75-79
    • Gleiter, H.M.1    Nugent, J.H.A.2    Haag, E.3    Renger, G.4
  • 62
    • 0032885987 scopus 로고    scopus 로고
    • Iron and activated oxygen species in biology: The basic chemistry
    • Pierre, J. L., and Fontecave, M. (1999) Iron and activated oxygen species in biology: the basic chemistry, Biometals 12, 195-199.
    • (1999) Biometals , vol.12 , pp. 195-199
    • Pierre, J.L.1    Fontecave, M.2
  • 63
    • 0000337384 scopus 로고    scopus 로고
    • 559
    • (Ort, D. R., Yocum, C. F., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 559, in Oxygenic Photosynthesis: The Light Reactions (Ort, D. R., Yocum, C. F., Eds.) Vol. 4, pp 249-264, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , vol.4 , pp. 249-264
    • Whitmarsh, J.1    Pakrasi, H.2
  • 64
    • 0023953589 scopus 로고
    • Redox and acid-base characterization of cytochrome b559 in photosystem II particles
    • Ortega, J. M., Hervas, M., and Losada, M. (1988) Redox and acid-base characterization of cytochrome b559 in photosystem II particles, Eur. J. Biochem. 171, 449-455.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 449-455
    • Ortega, J.M.1    Hervas, M.2    Losada, M.3
  • 67
    • 0344276747 scopus 로고
    • Structure and function of photosystem II reaction center
    • (Murata, N., Ed.), Kluwer Academic Publisher, Dordrecht, The Netherlands
    • Satoh, K. (1992) Structure and Function of Photosystem II Reaction Center, in Research in Photosynthesis (Murata, N., Ed.) Vol. 2, pp 3-12, Kluwer Academic Publisher, Dordrecht, The Netherlands.
    • (1992) Research in Photosynthesis , vol.2 , pp. 3-12
    • Satoh, K.1
  • 68
    • 0029127671 scopus 로고
    • Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: Implications for the mechanism of degradation of the D1 protein under illumination
    • Miyao, M., Ikeuchi, M., Yamamoto, N., and Ono, T. (1995) Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: implications for the mechanism of degradation of the D1 protein under illumination, Biochemistry 34, 10019-10026.
    • (1995) Biochemistry , vol.34 , pp. 10019-10026
    • Miyao, M.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.4
  • 69
    • 0000467762 scopus 로고    scopus 로고
    • 559 in intact chloroplasts with a new type of LED Array Spectrophotometer
    • 559 in intact chloroplasts with a new type of LED Array Spectrophotometer, Photosynth. Res. 47, 187-197.
    • (1996) Photosynth. Res. , vol.47 , pp. 187-197
    • Heimann, S.1    Schreiber, U.2
  • 71
  • 73
    • 0034646208 scopus 로고    scopus 로고
    • Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
    • Yeh, A. P., Hu, Y., Jenney, F. E., Jr., Adams, M. W. W., and Rees, D. C. (2000) Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states, Biochemistry 39, 2499-2508.
    • (2000) Biochemistry , vol.39 , pp. 2499-2508
    • Yeh, A.P.1    Hu, Y.2    Jenney Jr., F.E.3    Adams, M.W.W.4    Rees, D.C.5
  • 74
    • 0037028549 scopus 로고    scopus 로고
    • Spectroscopic studies of Pyrococcus furiosus superoxide reductase: Implications for active-site structures and the catalytic mechanism
    • Clay, M. D., Jenney, F. E., Jr., Hagedoorn, P. L., George, G. N., Adams, M. W. W., and Johnson, M. K. (2002) Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism, J. Am. Chem. Soc. 124, 788-805.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 788-805
    • Clay, M.D.1    Jenney Jr., F.E.2    Hagedoorn, P.L.3    George, G.N.4    Adams, M.W.W.5    Johnson, M.K.6
  • 76
    • 0037386522 scopus 로고    scopus 로고
    • Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
    • Clay, M. D., Cosper, C. A., Jenney, F. E., Jr., Adams, M. W. W., Johnson, M. K. (2003) Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase, Proc. Natl. Acad. Sci. U.S.A. 100, 3796-3801.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3796-3801
    • Clay, M.D.1    Cosper, C.A.2    Jenney Jr., F.E.3    Adams, M.W.W.4    Johnson, M.K.5
  • 77
    • 0025099299 scopus 로고
    • Formation by NO of nitrosyl adducts of redox components of the Photosystem II reaction center. I. NO binds to the acceptor-side non-heme iron
    • Petrouleas, V., and Diner, B. A. (1990) Formation by NO of nitrosyl adducts of redox components of the Photosystem II reaction center. I. NO binds to the acceptor-side non-heme iron, Biochim. Biophys. Acta 1015, 131-140.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 131-140
    • Petrouleas, V.1    Diner, B.A.2


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