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Volumn 149, Issue 6, 2003, Pages 1513-1522

Response of a strict anaerobe to oxygen: Survival strategies in Desulfovibrio gigas

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CATALASE; CELL PROTEIN; GLUTATHIONE REDUCTASE; HEAT SHOCK PROTEIN 60; LACTIC ACID; NUCLEOSIDE TRIPHOSPHATASE; OXYGEN; SCAVENGER; SULFATE; SUPEROXIDE;

EID: 0038480736     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26155-0     Document Type: Review
Times cited : (63)

References (51)
  • 1
    • 0036941823 scopus 로고    scopus 로고
    • Superoxide scavenging by neelaredoxin: Dismutation and reduction activities in anaerobes
    • Abreu, I. A., Xavier, A. V., LeGall, J., Cabelli, D. E. & 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
  • 3
  • 4
    • 41049100518 scopus 로고
    • Spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F. Jr & Sizer, I. W. (1952). Spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195, 133-140.
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers R.F., Jr.1    Sizer, I.W.2
  • 5
    • 0027505025 scopus 로고
    • Overexpression of YAP2, coding for a new yAP protein, and YAP1 in Saccharomyces cerevisiae alleviates growth inhibition caused by 1,10-phenanthroline
    • Bossier, P., Fernandes, L., Rocha, D. & Rodrigues-Pousada, C. (1993). Overexpression of YAP2, coding for a new yAP protein, and YAP1 in Saccharomyces cerevisiae alleviates growth inhibition caused by 1,10-phenanthroline. J Biol Chem 31, 23640-23645.
    • (1993) J. Biol. Chem. , vol.31 , pp. 23640-23645
    • Bossier, P.1    Fernandes, L.2    Rocha, D.3    Rodrigues-Pousada, C.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0027197351 scopus 로고
    • Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas
    • Chen, M., Liu, M.-Y., LeGall, J., Fareleira, P., Santos, H. & Xavier, A. V. (1993a). 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, M.1    Liu, M.-Y.2    LeGall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 8
    • 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, M., Liu, M.-Y., LeGall, J., Fareleira, P., Santos, H. & Xavier, A. V. (1993b). 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, M.1    Liu, M.-Y.2    LeGall, J.3    Fareleira, P.4    Santos, H.5    Xavier, A.V.6
  • 10
    • 0033758905 scopus 로고    scopus 로고
    • Oxygen respiration by Desulfovibrio species
    • Cypionka, H. (2000). Oxygen respiration by Desulfovibrio species. Annu Rev Microbiol 54, 827-848.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 827-848
    • Cypionka, H.1
  • 12
    • 0025168418 scopus 로고
    • Aerobic respiration in sulphate-reducing bacteria
    • Dilling, W. & Cypionka, H. (1990). Aerobic respiration in sulphate-reducing bacteria. FEMS Microbiol Lett 71, 123-128.
    • (1990) FEMS Microbiol. Lett. , vol.71 , pp. 123-128
    • Dilling, W.1    Cypionka, H.2
  • 13
    • 0033958343 scopus 로고    scopus 로고
    • Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas
    • Dos Santos, W. G., Pacheco, I., Liu, M.-Y., Teixeira, M., Xavier, A. V. & LeGall, J. (2000). Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas. J Bacteriol 182, 769-804.
    • (2000) J. Bacteriol. , vol.182 , pp. 769-804
    • Dos Santos, W.G.1    Pacheco, I.2    Liu, M.-Y.3    Teixeira, M.4    Xavier, A.V.5    LeGall, J.6
  • 14
    • 0030924390 scopus 로고    scopus 로고
    • Pathways for utilization of carbon reserves in Desulfovibrio gigas under fermentative and respiratory conditions
    • Fareleira, P., LeGall, J., Xavier, A. V. & Santos, H. (1997). Pathways for utilization of carbon reserves in Desulfovibrio gigas under fermentative and respiratory conditions. J Bacteriol 179, 3972-3980.
    • (1997) J. Bacteriol. , vol.179 , pp. 3972-3980
    • Fareleira, P.1    LeGall, J.2    Xavier, A.V.3    Santos, H.4
  • 15
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S. B. & Kogoma, T. (1991). Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev 55, 561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 16
    • 0033767236 scopus 로고    scopus 로고
    • Structure of a dioxygen reduction enzyme from Desulfovibrio gigas
    • & 11 other authors
    • Frazão, C., Silva, G., Gomes, C. M. & 11 other authors (2000). Structure of a dioxygen reduction enzyme from Desulfovibrio gigas. Nat Struct Biol 7, 1041-1045.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1041-1045
    • Frazão, C.1    Silva, G.2    Gomes, C.M.3
  • 17
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • Fridovich, I. (1983). Superoxide radical: an endogenous toxicant. Annu Rev Pharmacol Toxicol 23, 239-257.
    • (1983) Annu. Rev. Pharmacol. Toxicol. , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 18
    • 0025198891 scopus 로고
    • Survival of sulphate-reducing bacteria in oxic surface sediment of a seawater lake
    • Fukui, M. & Takii, S. (1990), Survival of sulphate-reducing bacteria in oxic surface sediment of a seawater lake. FEMS Microbiol Ecol 73, 317-322.
    • (1990) FEMS Microbiol. Ecol. , vol.73 , pp. 317-322
    • Fukui, M.1    Takii, S.2
  • 19
    • 0001528839 scopus 로고
    • Glutathione reductase
    • 3rd edn, Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie
    • Goldberg, D. M. & Spooner, R. (1983). Glutathione reductase. In Methods of Enzymatic Analysis, 3rd edn, vol. III, pp. 258-265. Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 258-265
    • Goldberg, D.M.1    Spooner, R.2
  • 20
    • 0029095434 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): The state of the art and the controversy of vertical versus horizontal systems
    • Görg, A., Boguth, G., Obermaier, C., Posch, A. & Weiss, W. (1995). Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): the state of the art and the controversy of vertical versus horizontal systems. Electrophoresis 16, 1079-1086.
    • (1995) Electrophoresis , vol.16 , pp. 1079-1086
    • Görg, A.1    Boguth, G.2    Obermaier, C.3    Posch, A.4    Weiss, W.5
  • 21
    • 0002125420 scopus 로고
    • Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulphate-reducing bacteria
    • Edited by A. M. Michelson, J. M. McCord & I. Fridovich. London: Academic Press
    • Hatchikian, E. C., LeGall, J. & Bell, G. R. (1977). Significance of superoxide dismutase and catalase activities in the strict anaerobes, sulphate-reducing bacteria. In Superoxide and Superoxide Dismutase, pp. 159-172. Edited by A. M. Michelson, J. M. McCord & I. Fridovich. London: Academic Press.
    • (1977) Superoxide and Superoxide Dismutase , pp. 159-172
    • Hatchikian, E.C.1    LeGall, J.2    Bell, G.R.3
  • 22
    • 0027288792 scopus 로고
    • Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas
    • Hensgens, C. M. H., Vonk, J., Vanbeeumen, J., Vanbruggen, E. F. J. & Hansen, T. A. (1993). Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas. J Bacteriol 175, 2859-2863.
    • (1993) J. Bacteriol. , vol.175 , pp. 2859-2863
    • Hensgens, C.M.H.1    Vonk, J.2    Vanbeeumen, J.3    Vanbruggen, E.F.J.4    Hansen, T.A.5
  • 23
    • 0016432892 scopus 로고
    • Superoxide dismutase in some obligatory anaerobic bacteria
    • Hewitt, J. & Morris, J. C. (1975). Superoxide dismutase in some obligatory anaerobic bacteria. FEBS Lett 50, 315-318.
    • (1975) FEBS Lett. , vol.50 , pp. 315-318
    • Hewitt, J.1    Morris, J.C.2
  • 24
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay, J. A. & Linn, S. (1988). DNA damage and oxygen radical toxicity. Science 240, 1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 25
    • 0002226697 scopus 로고
    • Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase
    • Kremer, D. R., Nienhuis-Kuiper, H. E. Timmer C. J. & Hansen, T. A. (1989). Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase. Arch Microbiol 151, 34-39.
    • (1989) Arch. Microbiol. , vol.151 , pp. 34-39
    • Kremer, D.R.1    Nienhuis-Kuiper, H.E.2    Timmer, C.J.3    Hansen, T.A.4
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T7
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T7. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0029869132 scopus 로고    scopus 로고
    • Anaerobes' response to oxygen: The sulphate-reducing bacteria
    • LeGall, J. & Xavier, A. V. (1996). Anaerobes' response to oxygen: the sulphate-reducing bacteria. Anaerobe 2, 1-9.
    • (1996) Anaerobe , vol.2 , pp. 1-9
    • LeGall, J.1    Xavier, A.V.2
  • 30
    • 0035805166 scopus 로고    scopus 로고
    • The "strict" anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain
    • Lemos, R. S., Gomes, C. M., Santana, M., LeGall, J., Xavier, A. V. & Teixeira, M. (2001). The "strict" anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain. FEBS Lett 496, 40-43.
    • (2001) FEBS Lett. , vol.496 , pp. 40-43
    • Lemos, R.S.1    Gomes, C.M.2    Santana, M.3    LeGall, J.4    Xavier, A.V.5    Teixeira, M.6
  • 31
    • 0035190269 scopus 로고    scopus 로고
    • Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: A novel oxidative stress protection system
    • Lumppio, H. L., Shenvi, N. V., Summers, A. O., Voordouw, G., & Kurtz, D. M., Jr (2001). Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system. J Bacteriol 183, 101-108.
    • (2001) J. Bacteriol. , vol.183 , pp. 101-108
    • Lumppio, H.L.1    Shenvi, N.V.2    Summers, A.O.3    Voordouw, G.4    Kurtz D.M., Jr.5
  • 32
    • 0031973278 scopus 로고    scopus 로고
    • Abundance and spatial organization of Gram-negative sulfate-reducing bacteria in activated sludge investigated by in situ probing with specific 16S rRNA targeted oligonucleotides
    • Manz, W., Eisenbrecher, M., Neu, T. R. & Szewzyk, U. (1998). Abundance and spatial organization of Gram-negative sulfate-reducing bacteria in activated sludge investigated by in situ probing with specific 16S rRNA targeted oligonucleotides. FEMS Microbiol Ecol 25, 43-61.
    • (1998) FEMS Microbiol. Ecol. , vol.25 , pp. 43-61
    • Manz, W.1    Eisenbrecher, M.2    Neu, T.R.3    Szewzyk, U.4
  • 33
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein
    • McCord, J. M. & Fridovich, I. (1969). Superoxide dismutase: an enzymic function for erythrocuprein. J Biol Chem 244, 6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 34
    • 0015056379 scopus 로고
    • An enzyme-based theory of obligate anaerobiosis: The physiological function of superoxide dismutase
    • McCord, J. M., Keele, B. B. & Fridovich, I. (1971). An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci U S A 68, 1024-1027.
    • (1971) Proc. Natl. Acad. Sci. U S A , vol.68 , pp. 1024-1027
    • McCord, J.M.1    Keele, B.B.2    Fridovich, I.3
  • 35
    • 0032864978 scopus 로고    scopus 로고
    • Unexpected population distribution in a microbial mat community: Sulfate-reducing bacteria localized to the highly oxic chemocline in contrast to a eukaryotic preference for anoxia
    • Minz, D., Fishbain, S., Green, S. J., Muyzer, G., Cohen, Y., Rittmann, B. E. & Stahl, D. A. (1999). Unexpected population distribution in a microbial mat community: sulfate-reducing bacteria localized to the highly oxic chemocline in contrast to a eukaryotic preference for anoxia. Appl Environ Microbiol 65, 4659-4665.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4659-4665
    • Minz, D.1    Fishbain, S.2    Green, S.J.3    Muyzer, G.4    Cohen, Y.5    Rittmann, B.E.6    Stahl, D.A.7
  • 36
    • 0015155688 scopus 로고
    • Oxygen and the growth and metabolism of Clostridium acetobutylicum
    • O'Brien, R. W. & Morris, J. G. (1971). Oxygen and the 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
  • 37
    • 0035062654 scopus 로고    scopus 로고
    • How does oxygen inhibit central metabolism in the obligate anaerobe Bacteroides thetaiotaomicron?
    • Pan, N. & Imlay, J. (2001). How does oxygen inhibit central metabolism in the obligate anaerobe Bacteroides thetaiotaomicron? Mol Microbiol 39, 1562-1571.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1562-1571
    • Pan, N.1    Imlay, J.2
  • 38
    • 0029848194 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobe, Bacteroides fragilis: A role for catalase in protection against hydrogen peroxide
    • Rocha, E. R., Selby, T., Coleman, J. P. & Smith, C. J. (1996). Oxidative stress response in an anaerobe, Bacteroides fragilis: a role for catalase in protection against hydrogen peroxide. J Bacteriol 178, 6895-6903.
    • (1996) J. Bacteriol. , vol.178 , pp. 6895-6903
    • Rocha, E.R.1    Selby, T.2    Coleman, J.P.3    Smith, C.J.4
  • 39
    • 0000600567 scopus 로고
    • Characterization of the improved sensitivity obtained using a flow method for oxygenating and mixing cell suspensions in NMR
    • Santos, H. & Turner, D. L. (1986). Characterization of the improved sensitivity obtained using a flow method for oxygenating and mixing cell suspensions in NMR. J Magn Reson 68, 345-349.
    • (1986) J. Magn. Reson. , vol.68 , pp. 345-349
    • Santos, H.1    Turner, D.L.2
  • 41
    • 0028674195 scopus 로고
    • In vivo nuclear magnetic resonance in study of physiology of sulfate-reducing bacteria
    • Santos, H., Fareleira, P., LeGall, J. & Xavier, A. V. (1994). In vivo nuclear magnetic resonance in study of physiology of sulfate-reducing bacteria. Methods Enzymol 243, 543-558.
    • (1994) Methods Enzymol. , vol.243 , pp. 543-558
    • Santos, H.1    Fareleira, P.2    LeGall, J.3    Xavier, A.V.4
  • 42
    • 0030744956 scopus 로고    scopus 로고
    • Vertical distribution of sulfate reducing bacteria at the oxic-anoxic interface of the oligotrophic Lake Stechlin
    • Sass, H., Cypionka, H. & Babenzien, H.-D. (1997). Vertical distribution of sulfate reducing bacteria at the oxic-anoxic interface of the oligotrophic Lake Stechlin. FEMS Microbiol Ecol 22, 245-255.
    • (1997) FEMS Microbiol. Ecol. , vol.22 , pp. 245-255
    • Sass, H.1    Cypionka, H.2    Babenzien, H.-D.3
  • 43
    • 0031848920 scopus 로고    scopus 로고
    • Psychrotolerant sulfate-reducing bacteria from an oxic freshwater sediment, description of Desulfovibrio cuneatus sp. nov. and Desulfovibrio litoralis sp. nov
    • Sass, H., Bertchold, M., Branke, J., Köning, H., Cypionka, H. & Babenzien, H.-D. (1998). Psychrotolerant sulfate-reducing bacteria from an oxic freshwater sediment, description of Desulfovibrio cuneatus sp. nov. and Desulfovibrio litoralis sp. nov. Syst Appl Microbiol 21, 212-219.
    • (1998) Syst. Appl. Microbiol. , vol.21 , pp. 212-219
    • Sass, H.1    Bertchold, M.2    Branke, J.3    Köning, H.4    Cypionka, H.5    Babenzien, H.-D.6
  • 44
    • 0034801545 scopus 로고    scopus 로고
    • Analysis of the Desulfovibrio gigas transcriptional unit containing rubredoxin (rd) and rubredoxin-oxygen oxidoreductase (roo) genes and upstream ORFs
    • Silva, G., Oliveira, S., LeGall, J., Xavier, A. V. & Rodrigues-Pousada, C. (2001a). Analysis of the Desulfovibrio gigas transcriptional unit containing rubredoxin (rd) and rubredoxin-oxygen oxidoreductase (roo) genes and upstream ORFs. Biochem Biophys Res Common 280, 491-502.
    • (2001) Biochem. Biophys. Res. Common. , vol.280 , pp. 491-502
    • Silva, G.1    Oliveira, S.2    LeGall, J.3    Xavier, A.V.4    Rodrigues-Pousada, C.5
  • 45
    • 0034938144 scopus 로고    scopus 로고
    • Molecular characterization of Desulfovibrio gigas neelaredoxin, a protein involved in oxygen detoxification in anaerobes
    • Silva, G., LeGall, J., Xavier, A. V., Teixeira, M. & Rodrigues-Pousada, C. (2001b). Molecular characterization of Desulfovibrio gigas neelaredoxin, a protein involved in oxygen detoxification in anaerobes. J Bacteriol 183, 4413-4420.
    • (2001) J. Bacteriol. , vol.183 , pp. 4413-4420
    • Silva, G.1    LeGall, J.2    Xavier, A.V.3    Teixeira, M.4    Rodrigues-Pousada, C.5
  • 46
    • 0020084735 scopus 로고
    • Oxygen-labile L(+)lactate dehydrogenase activity in Desulfovibrio desulfuricans
    • Stams, A. J. M. & Hansen, T. A. (1982). Oxygen-labile L(+)lactate dehydrogenase activity in Desulfovibrio desulfuricans. FEMS Microbiol Lett 13, 389-394.
    • (1982) FEMS Microbiol. Lett. , vol.13 , pp. 389-394
    • Stams, A.J.M.1    Hansen, T.A.2
  • 48
    • 0012456693 scopus 로고
    • Analysis of bacteriphage T7 early RNAs and proteins on slab gels
    • Studier, F. W. (1973). Analysis of bacteriphage T7 early RNAs and proteins on slab gels. J Mol Biol 79, 237-248.
    • (1973) J. Mol. Biol. , vol.79 , pp. 237-248
    • Studier, F.W.1
  • 50
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze, F. (1969). Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 27, 502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1


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