메뉴 건너뛰기




Volumn 159, Issue PART 12, 2013, Pages 2663-2673

Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: Roles in oxygen defence and electron link with periplasmic hydrogen oxidation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; HYDROGEN; LACTIC ACID; MENADIOL; OXIDOREDUCTASE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84888869356     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.071282-0     Document Type: Article
Times cited : (45)

References (52)
  • 1
    • 0025287571 scopus 로고
    • Effects of the oxygen on the growth of Desulfovibrio desulfuricans
    • Abdollahi, H. & Wimpenny, J. (1990). Effects of the oxygen on the growth of Desulfovibrio desulfuricans. J Gen Microbiol 136, 1025-1030.
    • (1990) J Gen Microbiol , vol.136 , pp. 1025-1030
    • Abdollahi, H.1    Wimpenny, J.2
  • 3
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • Baughn, A. D. & Malamy, M. H. (2004). The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen. Nature 427, 441-444.
    • (2004) Nature , vol.427 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 58449135158 scopus 로고    scopus 로고
    • The multiple evolutionary histories of dioxygen reductases: Implications for the origin and evolution of aerobic respiration
    • Brochier-Armanet, C., Talla, E. & Gribaldo, S. (2009). The multiple evolutionary histories of dioxygen reductases: implications for the origin and evolution of aerobic respiration. Mol Biol Evol 26, 285-297.
    • (2009) Mol Biol Evol , vol.26 , pp. 285-297
    • Brochier-Armanet, C.1    Talla, E.2    Gribaldo, S.3
  • 8
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana, J., Lübben, M., Saraste, M. & Higgins, D. G. (1994). Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J 13, 2516-2525.
    • (1994) EMBO J , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lübben, M.2    Saraste, M.3    Higgins, D.G.4
  • 9
    • 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
  • 10
    • 0002364807 scopus 로고
    • Survival of sulfatereducing bacteria after oxygen stress, and growth in sulfate-free oxygen sulfide gradients
    • Cypionka, H., Widdel, F. & Pfennig, N. (1985). Survival of sulfatereducing bacteria after oxygen stress, and growth in sulfate-free oxygen sulfide gradients. FEMS Microbiol Ecol 31, 39-45.
    • (1985) FEMS Microbiol Ecol , vol.31 , pp. 39-45
    • Cypionka, H.1    Widdel, F.2    Pfennig, N.3
  • 11
    • 0033851906 scopus 로고    scopus 로고
    • Deletion of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough hampers hydrogen metabolism and low-redoxpotential niche establishment
    • Dolla, A., Pohorelic, B. K., Voordouw, J. K. & Voordouw, G. (2000). Deletion of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough hampers hydrogen metabolism and low-redoxpotential niche establishment. Arch Microbiol 174, 143-151.
    • (2000) Arch Microbiol , vol.174 , pp. 143-151
    • Dolla, A.1    Pohorelic, B.K.2    Voordouw, J.K.3    Voordouw, G.4
  • 12
    • 0000652490 scopus 로고
    • A study on electron transportdriven proton translocation in Desulfovibrio desulfuricans
    • Fitz, R. M. & Cypionka, H. (1989). A study on electron transportdriven proton translocation in Desulfovibrio desulfuricans. Arch Microbiol 152, 369-376.
    • (1989) Arch Microbiol , vol.152 , pp. 369-376
    • Fitz, R.M.1    Cypionka, H.2
  • 13
    • 0347899391 scopus 로고    scopus 로고
    • A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress
    • Fournier, M., Dermoun, Z., Durand, M. C. & Dolla, A. (2004). A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress. J Biol Chem 279, 1787-1793.
    • (2004) J Biol Chem , vol.279 , pp. 1787-1793
    • Fournier, M.1    Dermoun, Z.2    Durand, M.C.3    Dolla, A.4
  • 15
    • 0030837663 scopus 로고    scopus 로고
    • Targeted gene-replacement mutagenesis of dcrA, encoding an oxygen sensor of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Fu, R. & Voordouw, G. (1997). Targeted gene-replacement mutagenesis of dcrA, encoding an oxygen sensor of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Microbiology 143, 1815-1826.
    • (1997) Microbiology , vol.143 , pp. 1815-1826
    • Fu, R.1    Voordouw, G.2
  • 16
    • 77955236947 scopus 로고    scopus 로고
    • Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus
    • Gao, X., Xin, Y., Bell, P. D., Wen, J. & Blankenship, R. E. (2010). Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus. Biochemistry 49, 6670-6679.
    • (2010) Biochemistry , vol.49 , pp. 6670-6679
    • Gao, X.1    Xin, Y.2    Bell, P.D.3    Wen, J.4    Blankenship, R.E.5
  • 17
    • 84857913190 scopus 로고    scopus 로고
    • Cytochrome bd oxidase and nitric oxide: From reaction mechanisms to bacterial physiology
    • Giuffrè, A., Borisov, V. B., Mastronicola, D., Sarti, P. & Forte, E. (2012). Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology. FEBS Lett 586, 622-629.
    • (2012) FEBS Lett , vol.586 , pp. 622-629
    • Giuffrè, A.1    Borisov, V.B.2    Mastronicola, D.3    Sarti, P.4    Forte, E.5
  • 18
    • 0024320468 scopus 로고
    • Direct electron transfer of redox proteins at the bare glassy carbon electrode
    • Hagen, W. R. (1989). Direct electron transfer of redox proteins at the bare glassy carbon electrode. Eur J Biochem 182, 523-530.
    • (1989) Eur J Biochem , vol.182 , pp. 523-530
    • Hagen, W.R.1
  • 20
    • 0036200881 scopus 로고    scopus 로고
    • Successional development of sulfate-reducing bacterial populations and their activities in a wastewater biofilm growing under microaerophilic conditions
    • Ito, T., Okabe, S., Satoh, H. & Watanabe, Y. (2002). Successional development of sulfate-reducing bacterial populations and their activities in a wastewater biofilm growing under microaerophilic conditions. Appl Environ Microbiol 68, 1392-1402.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 1392-1402
    • Ito, T.1    Okabe, S.2    Satoh, H.3    Watanabe, Y.4
  • 21
    • 0030812874 scopus 로고    scopus 로고
    • The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation
    • Juty, N. S., Moshiri, F., Merrick, M., Anthony, C. & Hill, S. (1997). The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation. Microbiology 143, 2673-2683.
    • (1997) Microbiology , vol.143 , pp. 2673-2683
    • Juty, N.S.1    Moshiri, F.2    Merrick, M.3    Anthony, C.4    Hill, S.5
  • 22
    • 0028859641 scopus 로고
    • A gene encoding a cytochrome c oxidase-like protein is located closely to the cytochrome c-553 gene in the anaerobic bacterium, Desulfovibrio vulgaris (Miyazaki F)
    • Kitamura, M., Mizugai, K., Taniguchi, M., Akutsu, H., Kumagai, I. & Nakaya, T. (1995). A gene encoding a cytochrome c oxidase-like protein is located closely to the cytochrome c-553 gene in the anaerobic bacterium, Desulfovibrio vulgaris (Miyazaki F). Microbiol Immunol 39, 75-80.
    • (1995) Microbiol Immunol , vol.39 , pp. 75-80
    • Kitamura, M.1    Mizugai, K.2    Taniguchi, M.3    Akutsu, H.4    Kumagai, I.5    Nakaya, T.6
  • 23
    • 1842779212 scopus 로고    scopus 로고
    • Oxygen tolerance of sulfate-reducing bacteria in activated sludge
    • Kjeldsen, K. U., Joulian, C. & Ingvorsen, K. (2004). Oxygen tolerance of sulfate-reducing bacteria in activated sludge. Environ Sci Technol 38, 2038-2043.
    • (2004) Environ Sci Technol , vol.38 , pp. 2038-2043
    • Kjeldsen, K.U.1    Joulian, C.2    Ingvorsen, K.3
  • 24
    • 0031931771 scopus 로고    scopus 로고
    • Strategies of sulfatereducing bacteria to escape oxygen stress in a cyanobacterial mat
    • Krekeler, D., Teske, A. & Cypionka, H. (1998). Strategies of sulfatereducing bacteria to escape oxygen stress in a cyanobacterial mat. FEMS Microbiol Ecol 25, 89-96.
    • (1998) FEMS Microbiol Ecol , vol.25 , pp. 89-96
    • Krekeler, D.1    Teske, A.2    Cypionka, H.3
  • 25
    • 80052366880 scopus 로고    scopus 로고
    • Oxygen reduction in the strict anaerobe Desulfovibrio vulgaris Hildenborough: Characterization of two membrane-bound oxygen reductases
    • Lamrabet, O., Pieulle, L., Aubert, C., Mouhamar, F., Stocker, P., Dolla, A. & Brasseur, G. (2011). Oxygen reduction in the strict anaerobe Desulfovibrio vulgaris Hildenborough: characterization of two membrane-bound oxygen reductases. Microbiology 157, 2720-2732.
    • (2011) Microbiology , vol.157 , pp. 2720-2732
    • Lamrabet, O.1    Pieulle, L.2    Aubert, C.3    Mouhamar, F.4    Stocker, P.5    Dolla, A.6    Brasseur, G.7
  • 26
    • 0035805166 scopus 로고    scopus 로고
    • The 'strict' anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chains
    • 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
  • 27
    • 56449103177 scopus 로고    scopus 로고
    • The haem-copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II
    • Lobo, S. A., Almeida, C. C., Carita, J. N., Teixeira, M. & Saraiva, L. M. (2008). The haem-copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II. Biochim Biophys Acta 1777, 1528-1534.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1528-1534
    • Lobo, S.A.1    Almeida, C.C.2    Carita, J.N.3    Teixeira, M.4    Saraiva, L.M.5
  • 28
    • 0027404899 scopus 로고
    • Influence of oxygen on sulphate reduction and growth on sulfate-reducing bacteria
    • Marschall, C., Frenzel, C. & Cypionka, H. (1993). Influence of oxygen on sulphate reduction and growth on sulfate-reducing bacteria. Arch Microbiol 159, 168-173.
    • (1993) Arch Microbiol , vol.159 , pp. 168-173
    • Marschall, C.1    Frenzel, C.2    Cypionka, H.3
  • 29
    • 14344250484 scopus 로고    scopus 로고
    • Diversity and vertical distribution of cultured and uncultured Deltaproteobacteria in an intertidal mud flat of the Wadden Sea
    • Mussmann, M., Ishii, K., Rabus, R. & Amann, R. (2005). Diversity and vertical distribution of cultured and uncultured Deltaproteobacteria in an intertidal mud flat of the Wadden Sea. Environ Microbiol 7, 405-418.
    • (2005) Environ Microbiol , vol.7 , pp. 405-418
    • Mussmann, M.1    Ishii, K.2    Rabus, R.3    Amann, R.4
  • 30
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira, M. M., Santana, M. & Teixeira, M. (2001). A novel scenario for the evolution of haem-copper oxygen reductases. Biochim Biophys Acta 1505, 185-208.
    • (2001) Biochim Biophys Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 31
    • 34948894523 scopus 로고    scopus 로고
    • The alternative complex III from Rhodothermus marinus-a prototype of a new family of quinol: Electron acceptor oxidoreductases
    • Pereira, M. M., Refojo, P. N., Hreggvidsson, G. O., Hjorleifsdottir, S. & Teixeira, M. (2007). The alternative complex III from Rhodothermus marinus-a prototype of a new family of quinol: electron acceptor oxidoreductases. FEBS Lett 581, 4831-4835.
    • (2007) FEBS Lett , vol.581 , pp. 4831-4835
    • Pereira, M.M.1    Refojo, P.N.2    Hreggvidsson, G.O.3    Hjorleifsdottir, S.4    Teixeira, M.5
  • 32
    • 30344465022 scopus 로고    scopus 로고
    • Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex-a membrane-bound redox complex involved in the sulfate respiratory pathway
    • Pires, R. H., Venceslau, S. S., Morais, F., Teixeira, M., Xavier, A. V. & Pereira, I. A. (2006). Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex-a membrane-bound redox complex involved in the sulfate respiratory pathway. Biochemistry 45, 249-262.
    • (2006) Biochemistry , vol.45 , pp. 249-262
    • Pires, R.H.1    Venceslau, S.S.2    Morais, F.3    Teixeira, M.4    Xavier, A.V.5    Pereira, I.A.6
  • 33
    • 0036669911 scopus 로고    scopus 로고
    • Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism
    • Pitcher, R. S., Brittain, T. & Watmough, N. J. (2002). Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism. Biochem Soc Trans 30, 653-658.
    • (2002) Biochem Soc Trans , vol.30 , pp. 653-658
    • Pitcher, R.S.1    Brittain, T.2    Watmough, N.J.3
  • 34
    • 0021104863 scopus 로고
    • Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins
    • Poole, R. K. (1983). Bacterial cytochrome oxidases. A structurally and functionally diverse group of electron-transfer proteins. Biochim Biophys Acta 726, 205-243.
    • (1983) Biochim Biophys Acta , vol.726 , pp. 205-243
    • Poole, R.K.1
  • 35
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii-roles of the terminal oxidases
    • Poole, R. K. & Hill, S. (1997). Respiratory protection of nitrogenase activity in Azotobacter vinelandii-roles of the terminal oxidases. Biosci Rep 17, 303-317.
    • (1997) Biosci Rep , vol.17 , pp. 303-317
    • Poole, R.K.1    Hill, S.2
  • 36
    • 0004233143 scopus 로고
    • 2nd edn. Cambridge, U.K.: Cambridge University Press
    • Postgate, J. (1984). The Sulphate-reducing Bacteria, 2nd edn. Cambridge, U.K.: Cambridge University Press.
    • (1984) The Sulphate-reducing Bacteria
    • Postgate, J.1
  • 37
    • 0033857193 scopus 로고    scopus 로고
    • Community structure, cellular rRNA content, and activity of sulfate-reducing bacteria in marine arctic sediments
    • Ravenschlag, K., Sahm, K., Knoblauch, C., Jørgensen, B. B. & Amann, R. (2000). Community structure, cellular rRNA content, and activity of sulfate-reducing bacteria in marine arctic sediments. Appl Environ Microbiol 66, 3592-3602.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3592-3602
    • Ravenschlag, K.1    Sahm, K.2    Knoblauch, C.3    Jørgensen, B.B.4    Amann, R.5
  • 38
    • 77953807360 scopus 로고    scopus 로고
    • The alternative complex III of Rhodothermus marinus and its structural and functional association with caa3 oxygen reductase
    • Refojo, P. N., Teixeira, M. & Pereira, M. M. (2010). The alternative complex III of Rhodothermus marinus and its structural and functional association with caa3 oxygen reductase. Biochim Biophys Acta 1797, 1477-1482.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1477-1482
    • Refojo, P.N.1    Teixeira, M.2    Pereira, M.M.3
  • 39
    • 84884675773 scopus 로고    scopus 로고
    • Structural composition of alternative complex III: Variations on the same theme
    • Refojo, P. N., Ribeiro, M. A., Calisto, F., Teixeira, M. & Pereira, M. M. (2013). Structural composition of alternative complex III: variations on the same theme. Biochim Biophys Acta 1827, 1378-1382.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 1378-1382
    • Refojo, P.N.1    Ribeiro, M.A.2    Calisto, F.3    Teixeira, M.4    Pereira, M.M.5
  • 40
    • 44649189139 scopus 로고    scopus 로고
    • Presence and expression of terminal oxygen reductases in strictly anaerobic sulfate-reducing bacteria isolated from salt-marsh sediments
    • Santana, M. (2008). Presence and expression of terminal oxygen reductases in strictly anaerobic sulfate-reducing bacteria isolated from salt-marsh sediments. Anaerobe 14, 145-156.
    • (2008) Anaerobe , vol.14 , pp. 145-156
    • Santana, M.1
  • 42
    • 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., Berchtold, M., Branke, J., König, H., Cypionka, H. & Babenzien, H. D. (1998a). 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    Berchtold, M.2    Branke, J.3    König, H.4    Cypionka, H.5    Babenzien, H.D.6
  • 43
    • 0031657332 scopus 로고    scopus 로고
    • High genetic and physiological diversity of sulfatereducing bacteria isolated from an oligotrophic lake sediment
    • Sass, H., Wieringa, E., Cypionka, H., Babenzien, H. D. & Overmann, J. (1998b). High genetic and physiological diversity of sulfatereducing bacteria isolated from an oligotrophic lake sediment. Arch Microbiol 170, 243-251.
    • (1998) Arch Microbiol , vol.170 , pp. 243-251
    • Sass, H.1    Wieringa, E.2    Cypionka, H.3    Babenzien, H.D.4    Overmann, J.5
  • 44
    • 78651378230 scopus 로고    scopus 로고
    • Isocyanides inhibit [Fe]-hydrogenase with very high affinity
    • Shima, S. & Ataka, K. (2011). Isocyanides inhibit [Fe]-hydrogenase with very high affinity. FEBS Lett 585, 353-356.
    • (2011) FEBS Lett , vol.585 , pp. 353-356
    • Shima, S.1    Ataka, K.2
  • 46
    • 84928593553 scopus 로고    scopus 로고
    • Energy metabolism and phylogenetic diversity of sulphate-reducing bacteria
    • 1st by L. L. Barton & W. A. Hamilton. Cambridge: Cambridge University Press
    • Thauer, R. K., Stackebrandt, E. & Hamilton, W. A. (2007). Energy metabolism and phylogenetic diversity of sulphate-reducing bacteria. In Sulphate-Reducing Bacteria, 1st pp. 1-38. Edited by L. L. Barton & W. A. Hamilton. Cambridge: Cambridge University Press.
    • (2007) Sulphate-Reducing Bacteria , pp. 1-38
    • Thauer, R.K.1    Stackebrandt, E.2    Hamilton, W.A.3
  • 47
    • 77954940178 scopus 로고    scopus 로고
    • The Qrc membrane complex, related to the alternative complex III, is a menaquinone reductase involved in sulfate respiration
    • Venceslau, S. S., Lino, R. R. & Pereira, I. A. (2010). The Qrc membrane complex, related to the alternative complex III, is a menaquinone reductase involved in sulfate respiration. J Biol Chem 285, 22774-22783.
    • (2010) J Biol Chem , vol.285 , pp. 22774-22783
    • Venceslau, S.S.1    Lino, R.R.2    Pereira, I.A.3
  • 48
    • 0024322748 scopus 로고
    • Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp oxamicus Monticello
    • Voordouw, G., Strang, J. D. & Wilson, F. R. (1989). Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio vulgaris subsp. oxamicus Monticello. J Bacteriol 171, 3881-3889.
    • (1989) J Bacteriol , vol.171 , pp. 3881-3889
    • Voordouw, G.1    Strang, J.D.2    Wilson, F.R.3
  • 49
    • 0014959126 scopus 로고
    • Menaquinone-6 in the strict anaerobes Desulfovibrio vulgaris and Desulfovibrio gigas
    • Weber, M. M., Matschiner, J. T. & Peck, H. D. (1970). Menaquinone-6 in the strict anaerobes Desulfovibrio vulgaris and Desulfovibrio gigas. Biochem Biophys Res Commun 38, 197-204.
    • (1970) Biochem Biophys Res Commun , vol.38 , pp. 197-204
    • Weber, M.M.1    Matschiner, J.T.2    Peck, H.D.3
  • 50
    • 33749004533 scopus 로고    scopus 로고
    • Rubredoxin: Oxygen oxidoreductase enhances survival of Desulfovibrio vulgaris Hildenborough under microaerophilic conditions
    • Wildschut, J. D., Lang, R. M., Voordouw, J. K. & Voordouw, G. (2006). Rubredoxin: oxygen oxidoreductase enhances survival of Desulfovibrio vulgaris Hildenborough under microaerophilic conditions. J Bacteriol 188, 6253-6260.
    • (2006) J Bacteriol , vol.188 , pp. 6253-6260
    • Wildschut, J.D.1    Lang, R.M.2    Voordouw, J.K.3    Voordouw, G.4
  • 52
    • 77955964940 scopus 로고    scopus 로고
    • Effect of the deletion of qmoABC and the promoter-distal gene encoding a hypothetical protein on sulfate reduction in Desulfovibrio vulgaris Hildenborough
    • Zane, G. M., Yen, H. C. & Wall, J. D. (2010). Effect of the deletion of qmoABC and the promoter-distal gene encoding a hypothetical protein on sulfate reduction in Desulfovibrio vulgaris Hildenborough. Appl Environ Microbiol 76, 5500-5509.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5500-5509
    • Zane, G.M.1    Yen, H.C.2    Wall, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.