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Volumn 278, Issue 3, 2011, Pages 442-451

Methanoferrodoxin represents a new class of superoxide reductase containing an iron-sulfur cluster

Author keywords

detoxification; iron sulfur protein; methanogenic archaea; oxygen radicals; superoxide dismutase

Indexed keywords

CYTOCHROME C; FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; IRON SULFUR PROTEIN; METHANOFERRODOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RUBREDOXIN; UNCLASSIFIED DRUG;

EID: 78751671220     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07964.x     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I, (1995) Superoxide radical and superoxide dismutases. Annu Rev Biochem 64, 97-112.
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 2
    • 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 JJ, Ravi N, Huynh BH, Liu MY, &, 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
  • 4
    • 36549086765 scopus 로고    scopus 로고
    • Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase
    • >Riebe O, Fischer RJ, &, Bahl H, (2007) Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase. FEBS Lett 581, 5605-5610.
    • (2007) FEBS Lett , vol.581 , pp. 5605-5610
    • Riebe, O.1    Fischer, R.J.2    Bahl, H.3
  • 5
    • 0033752865 scopus 로고    scopus 로고
    • Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: Superoxide scavenging by neelaredoxin
    • Abreu IA, Saraiva LM, Carita J, Huber H, Stetter KO, Cabelli D, &, 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
  • 6
    • 15444372151 scopus 로고    scopus 로고
    • In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
    • Grunden AM, Jenney FE Jr, Ma K, Ji M, Weinberg MV, &, Adams MW, (2005) In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus. Appl Environ Microbiol 71, 1522-1530.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1522-1530
    • Grunden, A.M.1    Jenney, Jr.F.E.2    Ma, K.3    Ji, M.4    Weinberg, M.V.5    Adams, M.W.6
  • 7
    • 74449083884 scopus 로고    scopus 로고
    • Reductive elimination of superoxide: Structure and mechanism of superoxide reductases
    • Pinto AF, Rodrigues JV, &, Teixeira M, (2010) Reductive elimination of superoxide: structure and mechanism of superoxide reductases. Biochim Biophys Acta 1804, 285-297.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 285-297
    • Pinto, A.F.1    Rodrigues, J.V.2    Teixeira, M.3
  • 9
    • 35949002126 scopus 로고    scopus 로고
    • Simultaneous methanogenesis and oxygen reduction by Methanobrevibacter cuticularis at low oxygen fluxes
    • Tholen A, Pester M, &, Brune A, (2007) Simultaneous methanogenesis and oxygen reduction by Methanobrevibacter cuticularis at low oxygen fluxes. FEMS Microbiol Ecol 62, 303-312.
    • (2007) FEMS Microbiol Ecol , vol.62 , pp. 303-312
    • Tholen, A.1    Pester, M.2    Brune, A.3
  • 10
    • 0014961734 scopus 로고
    • The utility of superoxide dismutase in studying free radical reactions. II. The mechanism of the mediation of cytochrome c reduction by a variety of electron carriers
    • McCord JM, &, Fridovich I, (1970) The utility of superoxide dismutase in studying free radical reactions. II. The mechanism of the mediation of cytochrome c reduction by a variety of electron carriers. J Biol Chem 245, 1374-1377.
    • (1970) J Biol Chem , vol.245 , pp. 1374-1377
    • McCord, J.M.1    Fridovich, I.2
  • 11
    • 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 JP, Cabelli DE, &, Kurtz DM Jr, (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 USA 100, 3802-3807.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3802-3807
    • Emerson, J.P.1    Cabelli, D.E.2    Kurtz, Jr.D.M.3
  • 12
    • 0041527233 scopus 로고    scopus 로고
    • Development of a sensitive gene expression reporter system and an inducible promoter-repressor system for Clostridium acetobutylicum
    • Girbal L, Mortier-Barriere I, Raynaud F, Rouanet C, Croux C, &, Soucaille P, (2003) Development of a sensitive gene expression reporter system and an inducible promoter-repressor system for Clostridium acetobutylicum. Appl Environ Microbiol 69, 4985-4988.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 4985-4988
    • Girbal, L.1    Mortier-Barriere, I.2    Raynaud, F.3    Rouanet, C.4    Croux, C.5    Soucaille, P.6
  • 13
    • 33846450248 scopus 로고    scopus 로고
    • High levels of expression of the iron-sulfur proteins phthalate dioxygenase and phthalate dioxygenase reductase in Escherichia coli
    • Jaganaman S, Pinto A, Tarasev M, &, Ballou DP, (2007) High levels of expression of the iron-sulfur proteins phthalate dioxygenase and phthalate dioxygenase reductase in Escherichia coli. Protein Expr Purif 52, 273-279.
    • (2007) Protein Expr Purif , vol.52 , pp. 273-279
    • Jaganaman, S.1    Pinto, A.2    Tarasev, M.3    Ballou, D.P.4
  • 14
    • 70449209570 scopus 로고
    • Determination of serum copper and iron in single small sample
    • Landers JW, &, Zak B, (1958) Determination of serum copper and iron in single small sample. Tech Bull Regist Med Technol 28, 98-100.
    • (1958) Tech Bull Regist Med Technol , vol.28 , pp. 98-100
    • Landers, J.W.1    Zak, B.2
  • 15
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert H, (1983) Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins. Anal Biochem 131, 373-378.
    • (1983) Anal Biochem , vol.131 , pp. 373-378
    • Beinert, H.1
  • 16
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord JM, &, Fridovich I, (1968) The reduction of cytochrome c by milk xanthine oxidase. J Biol Chem 243, 5753-5760.
    • (1968) J Biol Chem , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 17
    • 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, &, Niviere V, (2000) Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J Biol Chem 275, 115-121.
    • (2000) J Biol Chem , vol.275 , pp. 115-121
    • Lombard, M.1    Fontecave, M.2    Touati, D.3    Niviere, V.4
  • 18
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, &, Fridovich I, (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44, 276-287.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 19
    • 0036941823 scopus 로고    scopus 로고
    • Superoxide scavenging by neelaredoxin: Dismutation and reduction activities in anaerobes
    • Abreu IA, Xavier AV, LeGall J, Cabelli DE, &, Teixeira M, (2002) Superoxide scavenging by neelaredoxin: dismutation and reduction activities in anaerobes. J Biol Inorg Chem 7, 668-674.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 668-674
    • Abreu, I.A.1    Xavier, A.V.2    Legall, J.3    Cabelli, D.E.4    Teixeira, M.5
  • 20
    • 0036940990 scopus 로고    scopus 로고
    • What is the ultimate fate of superoxide anion in vivo?
    • Auchere F, &, Rusnak F, (2002) What is the ultimate fate of superoxide anion in vivo? J Biol Inorg Chem 7, 664-667.
    • (2002) J Biol Inorg Chem , vol.7 , pp. 664-667
    • Auchere, F.1    Rusnak, F.2
  • 22
    • 0037028549 scopus 로고    scopus 로고
    • Spectroscopic studies of Pyrococcus furiosus superoxide reductase: Implications for active-site structures and the catalytic mechanism
    • Clay MD, Jenney FE Jr, Hagedoorn PL, George GN, Adams MW, &, Johnson MK, (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
  • 23
    • 0042155690 scopus 로고    scopus 로고
    • Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris
    • Clay MD, Emerson JP, Coulter ED, Kurtz DM Jr, &, Johnson MK, (2003) Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris. J Biol Inorg Chem 8, 671-682.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 671-682
    • Clay, M.D.1    Emerson, J.P.2    Coulter, E.D.3    Kurtz, Jr.D.M.4    Johnson, M.K.5
  • 25
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney FE Jr, Verhagen MF, Cui X, &, Adams MW, (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
  • 27
    • 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, Niviere V, Molina-Heredia FP, &, Bourgeois D, (2004) Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction. Structure 12, 1729-1740.
    • (2004) Structure , vol.12 , pp. 1729-1740
    • Adam, V.1    Royant, A.2    Niviere, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 28
    • 0034646208 scopus 로고    scopus 로고
    • Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
    • Yeh AP, Hu Y, Jenney FE Jr, Adams MW, &, Rees DC, (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
  • 29
    • 0037072267 scopus 로고    scopus 로고
    • Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: A FTIR study
    • Berthomieu C, Dupeyrat F, Fontecave M, Vermeglio A, &, Niviere V, (2002) Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study. Biochemistry 41, 10360-10368.
    • (2002) Biochemistry , vol.41 , pp. 10360-10368
    • Berthomieu, C.1    Dupeyrat, F.2    Fontecave, M.3    Vermeglio, A.4    Niviere, V.5
  • 32
    • 0026691441 scopus 로고
    • Characterization of cytochromes from Methanosarcina strain Gol and their involvement in electron transport during growth on methanol
    • Kamlage B, &, Blaut M, (1992) Characterization of cytochromes from Methanosarcina strain Gol and their involvement in electron transport during growth on methanol. J Bacteriol 174, 3921-3927.
    • (1992) J Bacteriol , vol.174 , pp. 3921-3927
    • Kamlage, B.1    Blaut, M.2
  • 33
    • 0035985581 scopus 로고    scopus 로고
    • How oxygen damages microbes: Oxygen tolerance and obligate anaerobiosis
    • Imlay JA, (2002) How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Adv Microb Physiol 46, 111-153.
    • (2002) Adv Microb Physiol , vol.46 , pp. 111-153
    • Imlay, J.A.1
  • 34
    • 0035685613 scopus 로고    scopus 로고
    • Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family
    • Zhao T, Cruz F, &, Ferry JG, (2001) Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family. J Bacteriol 183, 6225-6233.
    • (2001) J Bacteriol , vol.183 , pp. 6225-6233
    • Zhao, T.1    Cruz, F.2    Ferry, J.G.3
  • 36
    • 70349468045 scopus 로고    scopus 로고
    • Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri
    • Kulkarni G, Kridelbaugh DM, Guss AM, &, Metcalf WW, (2009) Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri. Proc Natl Acad Sci USA 106, 15915-15920.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15915-15920
    • Kulkarni, G.1    Kridelbaugh, D.M.2    Guss, A.M.3    Metcalf, W.W.4
  • 37
    • 0036357283 scopus 로고    scopus 로고
    • The unique biochemistry of methanogenesis
    • Deppenmeier U, (2002) The unique biochemistry of methanogenesis. Prog Nucleic Acid Res Mol Biol 71, 223-283.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 223-283
    • Deppenmeier, U.1
  • 38
    • 0032925305 scopus 로고    scopus 로고
    • Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri
    • Shima S, Netrusov A, Sordel M, Wicke M, Hartmann GC, &, Thauer RK, (1999) Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri. Arch Microbiol 171, 317-323.
    • (1999) Arch Microbiol , vol.171 , pp. 317-323
    • Shima, S.1    Netrusov, A.2    Sordel, M.3    Wicke, M.4    Hartmann, G.C.5    Thauer, R.K.6
  • 39
    • 0033850813 scopus 로고    scopus 로고
    • Protection of Methanosarcina barkeri against oxidative stress: Identification and characterization of an iron superoxide dismutase
    • Brioukhanov A, Netrusov A, Sordel M, Thauer RK, &, Shima S, (2000) Protection of Methanosarcina barkeri against oxidative stress: identification and characterization of an iron superoxide dismutase. Arch Microbiol 174, 213-216.
    • (2000) Arch Microbiol , vol.174 , pp. 213-216
    • Brioukhanov, A.1    Netrusov, A.2    Sordel, M.3    Thauer, R.K.4    Shima, S.5


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