메뉴 건너뛰기




Volumn 75, Issue 4, 2009, Pages 1021-1029

O2 and reactive oxygen species detoxification complex, composed of O2-responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in Clostridium acetobutylicum

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM ACETOBUTYLICUM; ELECTRON CARRIER PROTEINS; EXPRESSION LEVELS; FLOW CULTURE CONDITIONS; GENES ENCODING; HIGH AFFINITIES; NADH OXIDASE; OXIDOREDUCTASE; REACTIVE OXYGEN SPECIES; RUBREDOXIN; SUPEROXIDE REDUCTASE;

EID: 59949105355     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01425-08     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 33745763405 scopus 로고    scopus 로고
    • Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases
    • Auchère, F., S. R. Pauleta, P. Tavares, I. Moura, and J. J. Moura. 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
    • Auchère, F.1    Pauleta, S.R.2    Tavares, P.3    Moura, I.4    Moura, J.J.5
  • 2
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C., and I. Fridovich. 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
  • 3
    • 0027263895 scopus 로고
    • Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the "strict anaerobe" Desulfovibrio gigas
    • Chen, L., M. Y. Liu, J. Legall, P. Fareleira, H. Santos, and A. V. Xavier. 1993. Rubredoxin oxidase, a new flavo-hemo-protein, is the site of oxygen reduction to water by the "strict anaerobe" Desulfovibrio gigas. Biochem. Biophys. Res. Commun. 193:100-105.
    • (1993) Biochem. Biophys. Res. Commun , vol.193 , pp. 100-105
    • Chen, L.1    Liu, M.Y.2    Legall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 4
    • 0027197351 scopus 로고
    • Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas
    • Chen, L., M. Y. Liu, J. Legall, P. Fareleira, H. Santos, and A. V. Xavier. 1993. Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas. Eur. J. Biochem. 216:443-448.
    • (1993) Eur. J. Biochem , vol.216 , pp. 443-448
    • Chen, L.1    Liu, M.Y.2    Legall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 5
    • 0035119328 scopus 로고    scopus 로고
    • Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin
    • Das, A., E. D. Coulter, D. M. Kurtz, Jr., and L. G. Ljungdahl. 2001. Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin. J. Bacteriol. 183:1560-1567.
    • (2001) J. Bacteriol , vol.183 , pp. 1560-1567
    • Das, A.1    Coulter, E.D.2    Kurtz Jr., D.M.3    Ljungdahl, L.G.4
  • 6
    • 0014962562 scopus 로고
    • Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase
    • Fridovich, I. 1970. Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J. Biol. Chem. 245:4053-4057.
    • (1970) J. Biol. Chem , vol.245 , pp. 4053-4057
    • Fridovich, I.1
  • 7
    • 0030954667 scopus 로고    scopus 로고
    • Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin
    • Gomes, C. M., G. Silva, S. Oliveira, J. LeGall, M. Y. Liu, A. V. Xavier, C. Rodrigues-Pousada, and M. Teixeira. 1997. Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin. J. Biol. Chem. 272:22502-22508.
    • (1997) J. Biol. Chem , vol.272 , pp. 22502-22508
    • Gomes, C.M.1    Silva, G.2    Oliveira, S.3    LeGall, J.4    Liu, M.Y.5    Xavier, A.V.6    Rodrigues-Pousada, C.7    Teixeira, M.8
  • 8
    • 15444372151 scopus 로고    scopus 로고
    • In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
    • Grunden, A. M., F. E. Jenney, Jr., K. Ma, M. Ji, M. V. Weinberg, and M. W. Adams. 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
  • 9
    • 0034806268 scopus 로고    scopus 로고
    • Identification of the gene encoding NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum
    • Guedon, E., and H. Petitdemange. 2001. Identification of the gene encoding NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum. Biochem. Biophys. Res. Commun. 285:496-502.
    • (2001) Biochem. Biophys. Res. Commun , vol.285 , pp. 496-502
    • Guedon, E.1    Petitdemange, H.2
  • 10
    • 33645998098 scopus 로고    scopus 로고
    • The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a general stress protein
    • Hillmann, F., R. J. Fischer, and H. Bahl. 2006. The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a general stress protein. Arch. Microbiol. 185:270-276.
    • (2006) Arch. Microbiol , vol.185 , pp. 270-276
    • Hillmann, F.1    Fischer, R.J.2    Bahl, H.3
  • 11
    • 0003535096 scopus 로고    scopus 로고
    • 4th ed. Anaerobe laboratory, Virginia Polytechnic Institute and State University, Blacksburg, VA
    • Holdeman, L. V., E. P. Cato, and W. E. C. Moor. 1997. Anaerobe laboratory manual, 4th ed. Anaerobe laboratory, Virginia Polytechnic Institute and State University, Blacksburg, VA.
    • (1997) Anaerobe laboratory manual
    • Holdeman, L.V.1    Cato, E.P.2    Moor, W.E.C.3
  • 12
    • 1842703815 scopus 로고
    • Anaerobes and oxygen
    • K. T. Holland, J. S. Knapp, and J. G. Shoesmith ed, Chapman and Hall, New York, NY
    • Holland, K. T., J. S. Knapp, and J. G. Shoesmith. 1987. Anaerobes and oxygen, p. 4-12. In K. T. Holland, J. S. Knapp, and J. G. Shoesmith (ed.), Anaerobic bacteria. Chapman and Hall, New York, NY.
    • (1987) Anaerobic bacteria , pp. 4-12
    • Holland, K.T.1    Knapp, J.S.2    Shoesmith, J.G.3
  • 13
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, F. E., Jr., M. F. Verhagen, X. Cui, and M. W. Adams. 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
  • 15
    • 0031739172 scopus 로고    scopus 로고
    • Effect of oxygen on the growth of Clostridium butyricum (type species of the genus Clostridium), and the distribution of enzymes for oxygen and for active oxygen species in clostridia
    • Kawasaki, S., T. Nakagawa, Y. Nishiyama, Y. Benno, T. Uchimura, K. Komagata, K. Kozaki, and Y. Niimura. 1998. Effect of oxygen on the growth of Clostridium butyricum (type species of the genus Clostridium), and the distribution of enzymes for oxygen and for active oxygen species in clostridia. J. Ferment. Bioeng. 86:368-372.
    • (1998) J. Ferment. Bioeng , vol.86 , pp. 368-372
    • Kawasaki, S.1    Nakagawa, T.2    Nishiyama, Y.3    Benno, Y.4    Uchimura, T.5    Komagata, K.6    Kozaki, K.7    Niimura, Y.8
  • 16
    • 1842637847 scopus 로고    scopus 로고
    • 2O-forming NADH oxidase from Clostridium aminovalericum: Existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria
    • 2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. Arch. Microbiol. 181:324-330.
    • (2004) Arch. Microbiol , vol.181 , pp. 324-330
    • Kawasaki, S.1    Ishikura, J.2    Chiba, D.3    Nishino, T.4    Niimura, Y.5
  • 18
    • 29144523114 scopus 로고    scopus 로고
    • Adaptive responses to oxygen stress in obligatory anaerobes Clostridium acetobutylicum and Clostridium aminovalericum
    • Kawasaki, S., Y. Watamura, M. Ono, T. Watanabe, K. Takeda, and Y. Niimura. 2005. Adaptive responses to oxygen stress in obligatory anaerobes Clostridium acetobutylicum and Clostridium aminovalericum. Appl. Environ. Microbiol. 71:8442-8450.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 8442-8450
    • Kawasaki, S.1    Watamura, Y.2    Ono, M.3    Watanabe, T.4    Takeda, K.5    Niimura, Y.6
  • 20
    • 0034614443 scopus 로고    scopus 로고
    • Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity
    • Lombard, M., M. Fontecave, D. Touati, and V. Niviere. 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
  • 21
    • 0034282657 scopus 로고    scopus 로고
    • Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum
    • Lombard, M., D. Touati, M. Fontecave, and V. Niviere. 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
  • 22
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg, W., and B. E. Sobel. 1965. Rubredoxin: a new electron transfer protein from Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA 54:193-199.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.E.2
  • 23
    • 0032865879 scopus 로고    scopus 로고
    • A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Ma, K., and M. W. Adams. 1999. A hyperactive NAD(P)H:Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 181:5530-5533.
    • (1999) J. Bacteriol , vol.181 , pp. 5530-5533
    • Ma, K.1    Adams, M.W.2
  • 24
    • 4444328040 scopus 로고    scopus 로고
    • A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21
    • May, A., F. Hillmann, O. Riebe, R. J. Fischer, and H. Bahl. 2004. A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21. FEMS Microbiol. Lett. 238:249-254.
    • (2004) FEMS Microbiol. Lett , vol.238 , pp. 249-254
    • May, A.1    Hillmann, F.2    Riebe, O.3    Fischer, R.J.4    Bahl, H.5
  • 25
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and I. Fridovich. 1969. Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-6055.
    • (1969) J. Biol. Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 26
    • 0015056379 scopus 로고
    • An enzyme-based theory of obligate anaerobiosis: The physiological function of superoxide dismutase
    • McCord, J. M., B. B. Keele, Jr., and I. Fridovich. 1971. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. USA 68:1024-1027.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1024-1027
    • McCord, J.M.1    Keele Jr., B.B.2    Fridovich, I.3
  • 28
    • 0015155688 scopus 로고
    • Oxygen and growth and metabolism of Clostridium acetobutylicum
    • O'Brien, R. W., and J. G. Morris. 1971. Oxygen and growth and metabolism of Clostridium acetobutylicum. J. Gen. Microbiol. 68:307-318.
    • (1971) J. Gen. Microbiol , vol.68 , pp. 307-318
    • O'Brien, R.W.1    Morris, J.G.2
  • 29
    • 0018622764 scopus 로고
    • Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum
    • Petitdemange, H., R. Marczak, H. Blusson, and R. Gay. 1979. Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum. Biochem. Biophys. Res. Commun. 91:1258-1265.
    • (1979) Biochem. Biophys. Res. Commun , vol.91 , pp. 1258-1265
    • Petitdemange, H.1    Marczak, R.2    Blusson, H.3    Gay, R.4
  • 30
    • 36549086765 scopus 로고    scopus 로고
    • Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase
    • Riebe, O., R. J. Fischer, and H. Bahl. 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
  • 32
    • 0037452916 scopus 로고    scopus 로고
    • A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity
    • Silaghi-Dumitrescu, R., E. D. Coulter, A. Das, L. G. Ljungdahl, G. N. Jameson, B. H. Huynh, and D. M. Kurtz. 2003. A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity. Biochemistry 42:2806-2815.
    • (2003) Biochemistry , vol.42 , pp. 2806-2815
    • Silaghi-Dumitrescu, R.1    Coulter, E.D.2    Das, A.3    Ljungdahl, L.G.4    Jameson, G.N.5    Huynh, B.H.6    Kurtz, D.M.7
  • 33
    • 14644429695 scopus 로고    scopus 로고
    • Silaghi-Dumitrescu, R., K. Y. Ng, R. Viswanathan, and D. M. Kurtz, Jr. 2005. A flavo-diiron protein from Desulfovibrio vulgaris with oxidase and nitric oxide reductase activities. Evidence for an in vivo nitric oxide scavenging function. Biochemistry 44:3572-3579.
    • Silaghi-Dumitrescu, R., K. Y. Ng, R. Viswanathan, and D. M. Kurtz, Jr. 2005. A flavo-diiron protein from Desulfovibrio vulgaris with oxidase and nitric oxide reductase activities. Evidence for an in vivo nitric oxide scavenging function. Biochemistry 44:3572-3579.
  • 34
    • 0000738385 scopus 로고
    • Endospore-forming gram-positive rods and cocci
    • P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt ed, Williams and Wilkins Co, Baltimore, MD
    • Sneath, P. H. A. 1986. Endospore-forming gram-positive rods and cocci, p. 1104-1207. In P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology. Williams and Wilkins Co., Baltimore, MD.
    • (1986) Bergey's manual of systematic bacteriology , pp. 1104-1207
    • Sneath, P.H.A.1
  • 37
    • 0022991837 scopus 로고
    • Physiological responses of Bacteroides and Clostridium strains to environmental stress factors
    • Woods, D. R., and D. T. Jones. 1986. Physiological responses of Bacteroides and Clostridium strains to environmental stress factors. Adv. Microb. Physiol. 28:1-64.
    • (1986) Adv. Microb. Physiol , vol.28 , pp. 1-64
    • Woods, D.R.1    Jones, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.