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Volumn 438, Issue 3, 2011, Pages 485-494

New spectroscopic and electrochemical insights on a class I superoxide reductase: Evidence for an intramolecular electron-transfer pathway

Author keywords

Electron transfer; Non mediated electrochemistry; Reactive oxygen species (ROS); Superoxide reductase

Indexed keywords

IRON; OXIDOREDUCTASE; RUBREDOXIN; SUPEROXIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 80052149081     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110836     Document Type: Article
Times cited : (15)

References (43)
  • 2
    • 33645879244 scopus 로고    scopus 로고
    • Stalking intermediates in oxygen activation by iron enzymes: Motivation and method
    • Bollinger, Jr, J. M. and Krebs, C. (2006) Stalking intermediates in oxygen activation by iron enzymes: motivation and method. J. Inorg. Biochem. 100, 586-605
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 586-605
    • Bollinger Jr., J.M.1    Krebs, C.2
  • 3
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • Costas, M., Mehn, M. P., Jensen, M. P. and Que, Jr, L. (2004) Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem. Rev. 104, 939-986
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 4
    • 34547810057 scopus 로고    scopus 로고
    • Dioxygen activation at non-heme iron: Insights from rapid kinetic studies
    • Korendovych, I. V., Kryatov, S. V. and Rybak-Akimova, E. V. (2007) Dioxygen activation at non-heme iron: insights from rapid kinetic studies. Acc. Chem. Res. 40, 510-521
    • (2007) Acc. Chem. Res. , vol.40 , pp. 510-521
    • Korendovych, I.V.1    Kryatov, S.V.2    Rybak-Akimova, E.V.3
  • 5
    • 16244423655 scopus 로고    scopus 로고
    • Dioxygen activation by copper, heme and non-heme iron enzymes: Comparison of electronic structures and reactivities
    • Decker, A. and Solomon, E. I. (2005) Dioxygen activation by copper, heme and non-heme iron enzymes: comparison of electronic structures and reactivities. Curr. Opin. Chem. Biol. 9, 152-163
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 152-163
    • Decker, A.1    Solomon, E.I.2
  • 8
    • 0028673449 scopus 로고
    • Characterization of three proteins containing multiple iron sites: Rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster
    • Moura, I., Tavares, P. and Ravi, N. (1994) Characterization of three proteins containing multiple iron sites: rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster. Methods Enzymol. 243, 216-240
    • (1994) Methods Enzymol. , vol.243 , pp. 216-240
    • Moura, I.1    Tavares, P.2    Ravi, N.3
  • 10
    • 0025678997 scopus 로고
    • Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center
    • Moura, I., Tavares, P., Moura, J. J., Ravi, N., Huynh, B. H., Liu, M. Y. and LeGall, J. (1990) Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J. Biol. Chem. 265, 21596-21602
    • (1990) J. Biol. Chem. , vol.265 , pp. 21596-21602
    • Moura, I.1    Tavares, P.2    Moura, J.J.3    Ravi, N.4    Huynh, B.H.5    Liu, M.Y.6    LeGall, J.7
  • 11
    • 0038954602 scopus 로고    scopus 로고
    • Neelaredoxin from Pyrococcus furiosus is a novel type of superoxide dismutase
    • Jenney, F. E., Verhagen, M. and Adams, M. W. W. (1999) Neelaredoxin from Pyrococcus furiosus is a novel type of superoxide dismutase. J. Inorg. Biochem. 74, 181-181
    • (1999) J. Inorg. Biochem. , vol.74 , pp. 181-181
    • Jenney, F.E.1    Verhagen, M.2    Adams, M.W.W.3
  • 12
    • 0034282657 scopus 로고    scopus 로고
    • Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum
    • Lombard, M., Touati, D., Fontecave, M. and Niviere, V. (2000) Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum. J. Biol. Chem. 275, 27021-27026
    • (2000) J. Biol. Chem. , vol.275 , pp. 27021-27026
    • Lombard, M.1    Touati, D.2    Fontecave, M.3    Niviere, V.4
  • 13
    • 0033752865 scopus 로고    scopus 로고
    • Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: Superoxide scavenging by neelaredoxin
    • Abreu, I. A., Saraiva, L. M., Carita, J., Huber, H., Stetter, K. O., Cabelli, D. and Teixeira, M. (2000) Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin. Mol. Microbiol. 38, 322-334
    • (2000) Mol. Microbiol. , vol.38 , pp. 322-334
    • Abreu, I.A.1    Saraiva, L.M.2    Carita, J.3    Huber, H.4    Stetter, K.O.5    Cabelli, D.6    Teixeira, M.7
  • 14
    • 33846701126 scopus 로고    scopus 로고
    • Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: Comparison with neelaredoxin
    • Rodrigues, J. V., Saraiva, L. M., Abreu, I. A., Teixeira, M. and Cabelli, D. E. (2007) Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxin. J. Biol. Inorg. Chem. 12, 248-256
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 248-256
    • Rodrigues, J.V.1    Saraiva, L.M.2    Abreu, I.A.3    Teixeira, M.4    Cabelli, D.E.5
  • 15
    • 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, Jr, F. E., Adams, M. 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.4    Rees, D.C.5
  • 17
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, Jr, F. E., Verhagen, M. F., Cui, X. and Adams, M. 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.2    Cui, X.3    Adams, M.W.4
  • 18
    • 0024212517 scopus 로고
    • Superoxide dismutase: The first twenty years (1968-1988)
    • McCord, J. M. and Fridovich, I. (1988) Superoxide dismutase: the first twenty years (1968-1988). Free Radical Biol. Med. 5, 363-369
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 363-369
    • McCord, J.M.1    Fridovich, I.2
  • 20
    • 0029021221 scopus 로고
    • Expression of Desulfovibrio gigas desulforedoxin in Escherichia coli. Purification and characterization of mixed metal isoforms
    • Czaja, C., Litwiller, R., Tomlinson, A. J., Naylor, S., Tavares, P., LeGall, J., Moura, J. J., Moura, I. and Rusnak, F. (1995) Expression of Desulfovibrio gigas desulforedoxin in Escherichia coli. Purification and characterization of mixed metal isoforms. J. Biol. Chem. 270, 20273-20277
    • (1995) J. Biol. Chem. , vol.270 , pp. 20273-20277
    • Czaja, C.1    Litwiller, R.2    Tomlinson, A.J.3    Naylor, S.4    Tavares, P.5    LeGall, J.6    Moura, J.J.7    Moura, I.8    Rusnak, F.9
  • 21
    • 0029123025 scopus 로고
    • Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8Å resolution: A novel non-heme iron protein structure
    • Archer, M., Huber, R., Tavares, P., Moura, I., Moura, J. J., Carrondo, M. A., Sieker, L. C., LeGall, J. and Romao, M. J. (1995) Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8Å resolution: a novel non-heme iron protein structure. J. Mol. Biol. 251, 690-702
    • (1995) J. Mol. Biol. , vol.251 , pp. 690-702
    • Archer, M.1    Huber, R.2    Tavares, P.3    Moura, I.4    Moura, J.J.5    Carrondo, M.A.6    Sieker, L.C.7    LeGall, J.8    Romao, M.J.9
  • 22
    • 0029997030 scopus 로고    scopus 로고
    • Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins
    • DOI 10.1016/0014-5793(96)00364-X
    • Devreese, B., Tavares, P., Lampreia, J., Van Damme, N., Le Gall, J., Moura, J. J., Van Beeumen, J. and Moura, I. (1996) Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins. FEBS Lett. 385, 138-142 (Pubitemid 26169812)
    • (1996) FEBS Letters , vol.385 , Issue.3 , pp. 138-142
    • Devreese, B.1    Tavares, P.2    Lampreia, J.3    Van Damme, N.4    Le, G.J.5    Moura, J.J.G.6    Van Beeumen, J.7    Moura, I.8
  • 23
    • 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, Jr, F. E., Hagedoorn, P. L., George, G. N., Adams, M. 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.5    Johnson, M.K.6
  • 24
    • 8644259915 scopus 로고    scopus 로고
    • Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxin
    • Auchere, F., Sikkink, R., Cordas, C., Raleiras, P., Tavares, P., Moura, I. and Moura, J. J. (2004) Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the superoxide reductase neelaredoxin. J. Biol. Inorg. Chem. 9, 839-849
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 839-849
    • Auchere, F.1    Sikkink, R.2    Cordas, C.3    Raleiras, P.4    Tavares, P.5    Moura, I.6    Moura, J.J.7
  • 25
    • 28444470840 scopus 로고    scopus 로고
    • 3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes
    • 3+- hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes. J. Am. Chem. Soc. 127, 16436-16441
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16436-16441
    • Mathe, C.1    Niviere, V.2    Mattioli, T.A.3
  • 26
    • 17644398448 scopus 로고    scopus 로고
    • Rubredoxin acts as an electron donor for neelaredoxin in Archaeoglobus fulgidus
    • Rodrigues, J. V., Abreu, I. A., Saraiva, L. M. and Teixeira, M. (2005) Rubredoxin acts as an electron donor for neelaredoxin in Archaeoglobus fulgidus. Biochem. Biophys. Res. Commun. 329, 1300-1305
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 1300-1305
    • Rodrigues, J.V.1    Abreu, I.A.2    Saraiva, L.M.3    Teixeira, M.4
  • 28
    • 0037006991 scopus 로고    scopus 로고
    • Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris
    • DOI 10.1021/bi0119159
    • Emerson, J. P., Coulter, E. D., Cabelli, D. E., Phillips, R. S. and Kurtz, Jr, D. M. (2002) Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris. Biochemistry 41, 4348-4357 (Pubitemid 34259878)
    • (2002) Biochemistry , vol.41 , Issue.13 , pp. 4348-4357
    • Emerson, J.P.1    Coulter, E.D.2    Cabelli, D.E.3    Phillips, R.S.4    Kurtz Jr., D.M.5
  • 30
    • 0037389525 scopus 로고    scopus 로고
    • An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo
    • Emerson, J. P., Cabelli, D. E. and Kurtz, Jr, D. M. (2003) An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo. Proc. Natl. Acad. Sci. U.S.A. 100, 3802-3807
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3802-3807
    • Emerson, J.P.1    Cabelli, D.E.2    Kurtz Jr., D.M.3
  • 31
    • 33745763405 scopus 로고    scopus 로고
    • Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases
    • Auchere, F., Pauleta, S. R., Tavares, P., Moura, I. and Moura, J. J. (2006) Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases. J. Biol. Inorg. Chem. 11, 433-444
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 433-444
    • Auchere, F.1    Pauleta, S.R.2    Tavares, P.3    Moura, I.4    Moura, J.J.5
  • 33
    • 50849116758 scopus 로고    scopus 로고
    • Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced absorption spectroscopy
    • Wisitruangsakul, N., Zebger, I., Ly, K. H., Murgida, D. H., Ekgasit, S. and Hildebrandt, P. (2008) Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced absorption spectroscopy. Phys. Chem. Chem. Phys. 10, 5276-5286
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 5276-5286
    • Wisitruangsakul, N.1    Zebger, I.2    Ly, K.H.3    Murgida, D.H.4    Ekgasit, S.5    Hildebrandt, P.6
  • 37
    • 0037137649 scopus 로고    scopus 로고
    • Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes
    • Léger, C. J., Jones, A. K., Albracht, S. P. J. and Armstrong, F. A. (2002) Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and other enzymes. J. Phys. Chem. B. 106, 13058-13063
    • (2002) J. Phys. Chem. B. , vol.106 , pp. 13058-13063
    • Léger, C.J.1    Jones, A.K.2    Albracht, S.P.J.3    Armstrong, F.A.4
  • 38
    • 0000502040 scopus 로고
    • Factors influencing redox potentials of electron-transfer proteins
    • Moore, G. R., Pettigrew, G. W. and Rogers, N. K. (1986) Factors influencing redox potentials of electron-transfer proteins. Proc. Natl. Acad. Sci. U.S.A. 83, 4998-4999
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 4998-4999
    • Moore, G.R.1    Pettigrew, G.W.2    Rogers, N.K.3
  • 39
    • 49449092317 scopus 로고    scopus 로고
    • Conformational change detection in nonmetal proteins by direct electrochemical oxidation using diamond electrodes
    • Chiku, M., Nakamura, J., Fujishima, A. and Einaga, Y. (2008) Conformational change detection in nonmetal proteins by direct electrochemical oxidation using diamond electrodes. Anal. Chem. 80, 5783-5787
    • (2008) Anal. Chem. , vol.80 , pp. 5783-5787
    • Chiku, M.1    Nakamura, J.2    Fujishima, A.3    Einaga, Y.4
  • 40
    • 33746616396 scopus 로고    scopus 로고
    • Superoxide reduction mechanism of Archaeoglobus fulgidus one-iron superoxide reductase
    • DOI 10.1021/bi052489k
    • Rodrigues, J. V., Abreu, I. A., Cabelli, D. and Teixeira, M. (2006) Superoxide reduction mechanism of Archaeoglobus fulgidus one-iron superoxide reductase. Biochemistry 45, 9266-9278 (Pubitemid 44156390)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9266-9278
    • Rodrigues, J.V.1    Abreu, I.A.2    Cabelli, D.3    Teixeira, M.4
  • 41
    • 0035476428 scopus 로고    scopus 로고
    • A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
    • Coulter, E. D. and Kurtz, Jr, D. M. (2001) A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch. Biochem. Biophys. 394, 76-86
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 76-86
    • Coulter, E.D.1    Kurtz Jr., D.M.2
  • 42
    • 0033120861 scopus 로고    scopus 로고
    • Heme-mediated oxygen activation in biology: Cytochrome c oxidase and nitric oxide synthase
    • Poulos, T. L., Li, H. and Raman, C. S. (1999) Heme-mediated oxygen activation in biology: cytochrome c oxidase and nitric oxide synthase. Curr. Opin. Chem. Biol. 3, 131-137
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 131-137
    • Poulos, T.L.1    Li, H.2    Raman, C.S.3
  • 43
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X. and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4


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