메뉴 건너뛰기




Volumn 1787, Issue 8, 2009, Pages 985-994

Superoxide oxidase and reductase activity of cytochrome b559 in photosystem II

Author keywords

Cytochrome b559; Heme iron; Photosystem II; Superoxide oxidase; Superoxide reductase; Superoxide scavenger; Tris treated PSII membrane

Indexed keywords

ALPHA TOCOPHEROL; CYTOCHROME B559; CYTOCHROME C; DIETHYL PYROCARBONATE; HEME; HISTIDINE; IMIDAZOLE; IRON; OXIDOREDUCTASE; OXYGEN; SCAVENGER; SUPEROXIDE DISMUTASE; TROLOX C;

EID: 67649413283     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.03.017     Document Type: Article
Times cited : (34)

References (66)
  • 1
    • 0000337384 scopus 로고    scopus 로고
    • Form and function of cytochrome b-559
    • Ort D.R., and Yocum C. (Eds), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Whitmarsh J., and Pakrasi H.B. Form and function of cytochrome b-559. In: Ort D.R., and Yocum C. (Eds). Oxygenic Photosynthesis: The Light Reactions (1996), Kluwer Academic Publishers, Dordrecht, The Netherlands 249-264
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 249-264
    • Whitmarsh, J.1    Pakrasi, H.B.2
  • 3
    • 0022417647 scopus 로고
    • Axial ligands of chloroplast cytochrome b-559 - identification and requirement for a haem-cross-linked polypeptide structure
    • Babcock G.T., Widger W.R., Cramer W.A., Oertling W.A., and Metz J.G. Axial ligands of chloroplast cytochrome b-559 - identification and requirement for a haem-cross-linked polypeptide structure. Biochemistry 24 (1985) 3638-3645
    • (1985) Biochemistry , vol.24 , pp. 3638-3645
    • Babcock, G.T.1    Widger, W.R.2    Cramer, W.A.3    Oertling, W.A.4    Metz, J.G.5
  • 4
    • 0024298581 scopus 로고
    • Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product
    • Tae G.S., Black M.T., Cramer W.A., Vallon O., and Bogorad L. Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product. Biochemistry 27 (1988) 9075-9080
    • (1988) Biochemistry , vol.27 , pp. 9075-9080
    • Tae, G.S.1    Black, M.T.2    Cramer, W.A.3    Vallon, O.4    Bogorad, L.5
  • 5
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 A resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., and Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 A 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
  • 6
    • 0037422557 scopus 로고    scopus 로고
    • Crystal Structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution
    • Kamiya N., and Shen J.R. Crystal Structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 98-103
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 8
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 9
    • 0027965572 scopus 로고
    • Topography of the heme prosthetic group of cytochrome b559 in photosystem II reaction center
    • Tae G.S., and Cramer W.A. Topography of the heme prosthetic group of cytochrome b559 in photosystem II reaction center. Biochemistry 33 (1994) 10060-10068
    • (1994) Biochemistry , vol.33 , pp. 10060-10068
    • Tae, G.S.1    Cramer, W.A.2
  • 10
  • 11
    • 0033534159 scopus 로고    scopus 로고
    • Redox and spectral properties of cytochrome b559 in different preparations of photosystem II
    • Kaminskaya O., Kurreck J., Irrgang K.D., Renger G., and Shuvalov V. Redox and spectral properties of cytochrome b559 in different preparations of photosystem II. Biochemistry 38 (1999) 16223-16235
    • (1999) Biochemistry , vol.38 , pp. 16223-16235
    • Kaminskaya, O.1    Kurreck, J.2    Irrgang, K.D.3    Renger, G.4    Shuvalov, V.5
  • 12
    • 0033005863 scopus 로고    scopus 로고
    • Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions
    • Mizusawa N., Yamashita T., and Miyao M. Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions. Biochim. Biophys. Acta 1410 (1999) 273-286
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 273-286
    • Mizusawa, N.1    Yamashita, T.2    Miyao, M.3
  • 13
    • 0027179104 scopus 로고
    • The redox properties of cytochromes b imposed by the membrane electrostatic environment
    • Krishtalik L.I., Tae G.S., Cherepanov D.A., and Cramer W.A. The redox properties of cytochromes b imposed by the membrane electrostatic environment. Biophys. J. 65 (1993) 184-195
    • (1993) Biophys. J. , vol.65 , pp. 184-195
    • Krishtalik, L.I.1    Tae, G.S.2    Cherepanov, D.A.3    Cramer, W.A.4
  • 14
    • 0026454816 scopus 로고
    • Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared different spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds
    • Berthomieu C., Boussac A., Mantele W., Breton J., and Nabedryk E. Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared different spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds. Biochemistry 31 (1992) 11460-11471
    • (1992) Biochemistry , vol.31 , pp. 11460-11471
    • Berthomieu, C.1    Boussac, A.2    Mantele, W.3    Breton, J.4    Nabedryk, E.5
  • 15
    • 0034786927 scopus 로고    scopus 로고
    • Factors determining the special redox properties of photosynthetic cytochrome b559
    • Roncel M., Ortega J.M., and Losada M. Factors determining the special redox properties of photosynthetic cytochrome b559. Eur. J. Biochem 268 (2001) 4961-4968
    • (2001) Eur. J. Biochem , vol.268 , pp. 4961-4968
    • Roncel, M.1    Ortega, J.M.2    Losada, M.3
  • 16
    • 0001534244 scopus 로고
    • pH-dependent photoreactions of the high- and low-potential forms of cytochrome b559 in spinach PSII-enriched membranes
    • Ortega J.M., Hervás M., De la Rosa M.A., and Losada M. pH-dependent photoreactions of the high- and low-potential forms of cytochrome b559 in spinach PSII-enriched membranes. Photosynth. Res. 46 (1995) 185-191
    • (1995) Photosynth. Res. , vol.46 , pp. 185-191
    • Ortega, J.M.1    Hervás, M.2    De la Rosa, M.A.3    Losada, M.4
  • 17
    • 34249795159 scopus 로고    scopus 로고
    • Two reaction pathways for transformation of high potential cytochrome b559 of PS II into the intermediate potential form
    • Kaminskaya O., Shuvalov V., and Renger G. Two reaction pathways for transformation of high potential cytochrome b559 of PS II into the intermediate potential form. Biochim. Biophys. Acta 1767 (2007) 550-558
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 550-558
    • Kaminskaya, O.1    Shuvalov, V.2    Renger, G.3
  • 18
    • 33846617289 scopus 로고    scopus 로고
    • Evidence for a novel quinone binding site in the photosystem II complex that regulates the redox potential of cytochrome b559
    • Kaminskaya O., Shuvalov V., and Renger G. Evidence for a novel quinone binding site in the photosystem II complex that regulates the redox potential of cytochrome b559. Biochemistry, Biochemistry 46 (2007) 1091-1105
    • (2007) Biochemistry, Biochemistry , vol.46 , pp. 1091-1105
    • Kaminskaya, O.1    Shuvalov, V.2    Renger, G.3
  • 19
    • 0021347065 scopus 로고
    • The effect of herbicides on components of the PS II reaction centre measured by EPR
    • Rutherford A.W., Zimmermann J.L., and Mathis P. The effect of herbicides on components of the PS II reaction centre measured by EPR. FEBS Lett. 165 (1984) 156-162
    • (1984) FEBS Lett. , vol.165 , pp. 156-162
    • Rutherford, A.W.1    Zimmermann, J.L.2    Mathis, P.3
  • 21
    • 0000786567 scopus 로고
    • Restoration of high-potential cytochrome b559 in liposomes
    • Matsuda H., and Butler W.L. Restoration of high-potential cytochrome b559 in liposomes. Biochim. Biophys. Acta 725 (1983) 320-324
    • (1983) Biochim. Biophys. Acta , vol.725 , pp. 320-324
    • Matsuda, H.1    Butler, W.L.2
  • 22
    • 0033543222 scopus 로고    scopus 로고
    • Interconversion of low- and high-potential forms of cytochrome b559 in tris-washed photosystem II membranes under aerobic and anaerobic conditions
    • Gadjieva R., Mamedov F., Renger G., and Styring S. Interconversion of low- and high-potential forms of cytochrome b559 in tris-washed photosystem II membranes under aerobic and anaerobic conditions. Biochemistry 38 (1999) 10578-10589
    • (1999) Biochemistry , vol.38 , pp. 10578-10589
    • Gadjieva, R.1    Mamedov, F.2    Renger, G.3    Styring, S.4
  • 23
    • 34547814628 scopus 로고    scopus 로고
    • 559 in photosystem II depend on the integrity of the Mn cluster
    • 559 in photosystem II depend on the integrity of the Mn cluster. Physiol. Plant. 131 (2007) 41-49
    • (2007) Physiol. Plant. , vol.131 , pp. 41-49
    • Mamedov, F.1    Gadjieva, R.2    Styring, R.3
  • 24
    • 0003485891 scopus 로고    scopus 로고
    • The primary electron donor of photosystem II, p680, and photoinhibition
    • Ke B. (Ed), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Ke B. The primary electron donor of photosystem II, p680, and photoinhibition. In: Ke B. (Ed). Photosynthesis: Photobiochemistry and Photobiophysics (2001), Kluwer Academic Publishers, Dordrecht, The Netherlands 271-288
    • (2001) Photosynthesis: Photobiochemistry and Photobiophysics , pp. 271-288
    • Ke, B.1
  • 25
    • 0026722305 scopus 로고
    • Redox state of one electron component controls the rate of photoinhibition of photosystem II
    • Nedbal L., Samson G., and Whitmarsh J. Redox state of one electron component controls the rate of photoinhibition of photosystem II. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 7923-7929
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7923-7929
    • Nedbal, L.1    Samson, G.2    Whitmarsh, J.3
  • 26
    • 0027489759 scopus 로고
    • A functional model for the role of cytochrome b559 in the protection against donor and acceptor side photoinhibition
    • Barber J., and De Las Rivas J. A functional model for the role of cytochrome b559 in the protection against donor and acceptor side photoinhibition. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 10942-10946
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10942-10946
    • Barber, J.1    De Las Rivas, J.2
  • 27
    • 0028979602 scopus 로고
    • Evidence that cytochrome b559 protects photosystem II against photoinhibition
    • Poulson M., Samson G., and Whitmarsh J. Evidence that cytochrome b559 protects photosystem II against photoinhibition. Biochemistry 34 (1995) 10932-10938
    • (1995) Biochemistry , vol.34 , pp. 10932-10938
    • Poulson, M.1    Samson, G.2    Whitmarsh, J.3
  • 28
    • 0035808432 scopus 로고    scopus 로고
    • 559 in the presence of plastoquinones
    • 559 in the presence of plastoquinones. J. Biol. Chem. 276 (2001) 86-91
    • (2001) J. Biol. Chem. , vol.276 , pp. 86-91
    • Kruk, J.1    Strzalka, K.2
  • 33
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids
    • Kruk J., and Strzalka K. Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids. Photosynth. Res. 62 (1999) 273-279
    • (1999) Photosynth. Res. , vol.62 , pp. 273-279
    • Kruk, J.1    Strzalka, K.2
  • 35
    • 0027947679 scopus 로고
    • The Photoproduction of superoxide radicals and the superoxide-dismutase activity of photosystem II. The possible involvement of cytochrome b559
    • Ananyev G.M., Renger G., Wacker U., and Klimov V. The Photoproduction of superoxide radicals and the superoxide-dismutase activity of photosystem II. The possible involvement of cytochrome b559. Photosynth. Res. 41 (1994) 327-338
    • (1994) Photosynth. Res. , vol.41 , pp. 327-338
    • Ananyev, G.M.1    Renger, G.2    Wacker, U.3    Klimov, V.4
  • 36
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: oxygen detoxification without superoxide dismutase
    • Jenney F.E., Verhagen M.F.J.M., Cui X., and Adams M.W.W. Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286 (1999) 306-309
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney, F.E.1    Verhagen, M.F.J.M.2    Cui, X.3    Adams, M.W.W.4
  • 37
    • 0034614443 scopus 로고    scopus 로고
    • Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity
    • Lombard M., Fontecave M., Touati D., and Nivière V. Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J. Biol. Chem. 275 (2000) 115-121
    • (2000) J. Biol. Chem. , vol.275 , pp. 115-121
    • Lombard, M.1    Fontecave, M.2    Touati, D.3    Nivière, V.4
  • 39
    • 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., Adams M.W.W., and Rees D.C. Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states. Biochemistry 39 (2000) 2499-2508
    • (2000) Biochemistry , vol.39 , pp. 2499-2508
    • Yeh, A.P.1    Hu, Y.2    Jenney, F.E.3    Adams, M.W.W.4    Rees, D.C.5
  • 40
    • 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 Jr. F.E., Adams M.W.W., and Johnson M.K. Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 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
  • 41
    • 4444294012 scopus 로고    scopus 로고
    • Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
    • Adam V., Royant A., Nivière V., Molina-Heredia F.P., and Bourgeois D. Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction. Structure (London) 12 (2004) 5032-5040
    • (2004) Structure (London) , vol.12 , pp. 5032-5040
    • Adam, V.1    Royant, A.2    Nivière, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 42
    • 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. 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
  • 43
    • 0001625998 scopus 로고
    • Isolation of a photosystem II preparation from higher plants with highly enriched oxygen evolution activity
    • Ford R.C., and Evans M.C.W. Isolation of a photosystem II preparation from higher plants with highly enriched oxygen evolution activity. FEBS Lett. 160 (1983) 159-164
    • (1983) FEBS Lett. , vol.160 , pp. 159-164
    • Ford, R.C.1    Evans, M.C.W.2
  • 44
    • 0033167446 scopus 로고    scopus 로고
    • Characterization of the PsbX protein from Photosystem II and light regulation of its gene expression in higher plants
    • Shi L.X., Kim S.J., Marchant A., Robinson C., and Schröder W.P. Characterization of the PsbX protein from Photosystem II and light regulation of its gene expression in higher plants. Plant Mol. Biol. 40 (1999) 737-744
    • (1999) Plant Mol. Biol. , vol.40 , pp. 737-744
    • Shi, L.X.1    Kim, S.J.2    Marchant, A.3    Robinson, C.4    Schröder, W.P.5
  • 46
    • 0018115502 scopus 로고
    • Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer system
    • Dutton P.L. Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer system. Methods Enzymol. 54 (1978) 411-435
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 47
    • 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., and Tordo P. 2-ethoxycarbonyl-2-methyl-3,4-dihydro-2H-pyrrole-1-oxide: evaluation of the spin trapping properties. Free Radical Biol. Med. 28 (2000) 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
  • 49
    • 0000485416 scopus 로고
    • pH sensitivity of the redox state of cytochrome b559 may regulate its function as a protectant against donor and acceptor side photoinhibition
    • De Las Rivas J., Klein J., and Barber J. pH sensitivity of the redox state of cytochrome b559 may regulate its function as a protectant against donor and acceptor side photoinhibition. Photosynth. Res. 46 (1995) 193-202
    • (1995) Photosynth. Res. , vol.46 , pp. 193-202
    • De Las Rivas, J.1    Klein, J.2    Barber, J.3
  • 50
    • 0021103512 scopus 로고
    • 1H-NMR study on the tautomerism of the imidazole ring of histidine residues: I. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides
    • 1H-NMR study on the tautomerism of the imidazole ring of histidine residues: I. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides. Biochim. Biophys. Acta 742 (1983) 576-585
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 576-585
    • Tanokura, M.1
  • 51
    • 0021707174 scopus 로고
    • The effect of N,N′-dicyclohexylcarbodiimide on enzymes of bioenergetic relevance
    • Azzi A., Casey R.P., and Nalecz M.J. The effect of N,N′-dicyclohexylcarbodiimide on enzymes of bioenergetic relevance. Biochim. Biophys. Acta 768 (1984) 209-226
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 209-226
    • Azzi, A.1    Casey, R.P.2    Nalecz, M.J.3
  • 53
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • Wood P.M. The potential diagram for oxygen at pH 7. Biochem. J. 253 (1988) 287-289
    • (1988) Biochem. J. , vol.253 , pp. 287-289
    • Wood, P.M.1
  • 54
  • 55
    • 0036933628 scopus 로고    scopus 로고
    • The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo
    • Kurtz D.M., and Coulter E.D. The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo. J. Biol. Inorg. Chem. 7 (2002) 653-658
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 653-658
    • Kurtz, D.M.1    Coulter, E.D.2
  • 56
    • 33846292209 scopus 로고    scopus 로고
    • Understanding the mechanism of superoxide reductase (SOR)
    • Brines L.M., and Kovacs J.A. Understanding the mechanism of superoxide reductase (SOR). Eur. J. Inorg. Chem. 1 (2007) 29-38
    • (2007) Eur. J. Inorg. Chem. , vol.1 , pp. 29-38
    • Brines, L.M.1    Kovacs, J.A.2
  • 57
    • 0034624001 scopus 로고    scopus 로고
    • Copper- and zinc-containing superoxide dismutase can act as a superoxide reductase and a superoxide oxidase
    • Liochev S.I., and Fridovich I. Copper- and zinc-containing superoxide dismutase can act as a superoxide reductase and a superoxide oxidase. J. Biol. Chem. 275 (2000) 38482-38485
    • (2000) J. Biol. Chem. , vol.275 , pp. 38482-38485
    • Liochev, S.I.1    Fridovich, I.2
  • 60
    • 38949172029 scopus 로고    scopus 로고
    • Outer-sphere oxidation of the superoxide radical anion
    • Weinstock I. Outer-sphere oxidation of the superoxide radical anion. Inorg. Chem. 47 (2007) 404-406
    • (2007) Inorg. Chem. , vol.47 , pp. 404-406
    • Weinstock, I.1
  • 61
    • 33645893492 scopus 로고    scopus 로고
    • Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin
    • Kurtz D.M. Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin. J. Inorg. Biochem. 100 (2006) 679-693
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 679-693
    • Kurtz, D.M.1
  • 62
    • 0035942349 scopus 로고    scopus 로고
    • Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis
    • Lombard M., Houee-Levin C., Touati D., Fontecave M., and Nivière V. Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis. Biochemistry 40 (2001) 5032-5040
    • (2001) Biochemistry , vol.40 , pp. 5032-5040
    • Lombard, M.1    Houee-Levin, C.2    Touati, D.3    Fontecave, M.4    Nivière, V.5
  • 64
    • 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 Niviére V. Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii. J. Am. Chem. Soc. 124 (2002) 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    Niviére, V.7
  • 66
    • 34247525538 scopus 로고    scopus 로고
    • Raman spectroscopy confirmed the entrapment of iron(III)-peroxo intermediates in superoxide reductase crystals, which displayed different conformations/interactions within the crystallographic asymmetric unit
    • Katona G., Carpentier P., Nivière V., Amara P., Adam V., Ohana J., Tsanov N., and Bourgeois D. Raman spectroscopy confirmed the entrapment of iron(III)-peroxo intermediates in superoxide reductase crystals, which displayed different conformations/interactions within the crystallographic asymmetric unit. Science 316 (2007) 449-453
    • (2007) Science , vol.316 , pp. 449-453
    • Katona, G.1    Carpentier, P.2    Nivière, V.3    Amara, P.4    Adam, V.5    Ohana, J.6    Tsanov, N.7    Bourgeois, D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.