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Volumn 287, Issue 37, 2012, Pages 31165-31171

A bacterial electron-bifurcating hydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ACETOGENIC BACTERIA; ACID-LABILE; ATP SYNTHESIS; CARBON DIOXIDE FIXATION; EXPERIMENTAL DETERMINATION; HYDROGENASES; MULTIMERIC; REDUCTANTS;

EID: 84866142108     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.395038     Document Type: Article
Times cited : (175)

References (38)
  • 1
    • 0000491579 scopus 로고
    • + fixation in acetogenic bacteria: Variations on a theme
    • + fixation in acetogenic bacteria: variations on a theme. FEMS Microbiol. Rev. 39, 181-213
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 181-213
    • Fuchs, G.1
  • 2
    • 35148861695 scopus 로고    scopus 로고
    • On the origin of biochemistry at an alkaline hydrothermal vent
    • Martin, W., and Russell, M. J. (2007) On the origin of biochemistry at an alkaline hydrothermal vent. Philos. Trans. R. Soc. Lond. B Biol. Sci. 362, 1887-1925
    • (2007) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.362 , pp. 1887-1925
    • Martin, W.1    Russell, M.J.2
  • 3
    • 84857143067 scopus 로고    scopus 로고
    • Hydrogen, metals, bifurcating electrons, and proton gradients: The early evolution of biological energy conservation
    • Martin, W. F. (2012) Hydrogen, metals, bifurcating electrons, and proton gradients: the early evolution of biological energy conservation. FEBS Lett. 586, 485-493
    • (2012) FEBS Lett. , vol.586 , pp. 485-493
    • Martin, W.F.1
  • 5
    • 41349119857 scopus 로고    scopus 로고
    • Enzymology of the Wood-Ljungdahl pathway of acetogenesis
    • Ragsdale, S. W. (2008) Enzymology of the Wood-Ljungdahl pathway of acetogenesis. Ann. N.Y. Acad. Sci. 1125, 129-136
    • (2008) Ann. N.Y. Acad. Sci. , vol.1125 , pp. 129-136
    • Ragsdale, S.W.1
  • 7
    • 0003768271 scopus 로고
    • Drake, H. L., ed Chapman & Hall, New York
    • Ljungdahl, L. G. (1994) in Acetogenesis (Drake, H. L., ed) pp. 63-87, Chapman & Hall, New York
    • (1994) Acetogenesis , pp. 63-87
    • Ljungdahl, L.G.1
  • 9
    • 36549018651 scopus 로고    scopus 로고
    • Dissection of the caffeate respiratory chain in the acetogen Acetobacterium woodii: Indications for a Rnf-type NADH dehydrogenase as coupling site
    • Imkamp, F., Biegel, E., Jayamani, E., Buckel, W., and Müller, V. (2007) Dissection of the caffeate respiratory chain in the acetogen Acetobacterium woodii: indications for a Rnf-type NADH dehydrogenase as coupling site. J. Bacteriol. 189, 8145-8153
    • (2007) J. Bacteriol. , vol.189 , pp. 8145-8153
    • Imkamp, F.1    Biegel, E.2    Jayamani, E.3    Buckel, W.4    Müller, V.5
  • 11
    • 79951579402 scopus 로고    scopus 로고
    • Biochemistry, evolution, and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes
    • Biegel, E., Schmidt, S., González, J. M., and Müller, V. (2011) Biochemistry, evolution, and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes. Cell. Mol. Life Sci. 68, 613-634
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 613-634
    • Biegel, E.1    Schmidt, S.2    González, J.M.3    Müller, V.4
  • 12
    • 66649095357 scopus 로고    scopus 로고
    • Genetic, immunological, and biochemical evidence of a Rnf complex in the acetogen Acetobacterium woodii
    • Biegel, E., Schmidt, S., and Müller, V. (2009) Genetic, immunological, and biochemical evidence of a Rnf complex in the acetogen Acetobacterium woodii. Environ. Microbiol. 11, 1438-1443
    • (2009) Environ. Microbiol. , vol.11 , pp. 1438-1443
    • Biegel, E.1    Schmidt, S.2    Müller, V.3
  • 14
    • 34347387306 scopus 로고    scopus 로고
    • An intermediate step in the evolution of ATPases: The F1F0-ATPase from Acetobacterium woodii contains F-type and V-type rotor subunits and is capable of ATP synthesis
    • Fritz, M., and Müller, V. (2007) An intermediate step in the evolution of ATPases: the F1F0-ATPase from Acetobacterium woodii contains F-type and V-type rotor subunits and is capable of ATP synthesis. FEBS J. 274, 3421-3428
    • (2007) FEBS J. , vol.274 , pp. 3421-3428
    • Fritz, M.1    Müller, V.2
  • 16
    • 0002889025 scopus 로고
    • Occurrence of corrinoid-containing membrane proteins in anaerobic bacteria
    • Dangel, W., Schulz, H., Diekert, G., König, H., and Fuchs, G. (1987) Occurrence of corrinoid-containing membrane proteins in anaerobic bacteria. Arch. Microbiol. 148, 52-56
    • (1987) Arch. Microbiol. , vol.148 , pp. 52-56
    • Dangel, W.1    Schulz, H.2    Diekert, G.3    König, H.4    Fuchs, G.5
  • 17
    • 33744497825 scopus 로고    scopus 로고
    • Energy-converting [NiFe]-hydrogenases: More than just H2 activation
    • Hedderich, R., and Forzi, L. (2005) Energy-converting [NiFe]-hydrogenases: more than just H2 activation. J. Mol. Microbiol. Biotechnol. 10, 92-104
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.10 , pp. 92-104
    • Hedderich, R.1    Forzi, L.2
  • 18
    • 77955246393 scopus 로고    scopus 로고
    • Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei
    • Welte, C., Krätzer, C., and Deppenmeier, U. (2010) Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei. FEBS J. 277, 3396-3403
    • (2010) FEBS J. , vol.277 , pp. 3396-3403
    • Welte, C.1    Krätzer, C.2    Deppenmeier, U.3
  • 19
    • 0021527029 scopus 로고
    • Hydrogenase from Acetobacterium woodii
    • Ragsdale, S. W., and Ljungdahl, L. G. (1984) Hydrogenase from Acetobacterium woodii. Arch. Microbiol. 139, 361-365
    • (1984) Arch. Microbiol. , vol.139 , pp. 361-365
    • Ragsdale, S.W.1    Ljungdahl, L.G.2
  • 20
    • 38649099718 scopus 로고    scopus 로고
    • Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
    • Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel, W., and Thauer, R. K. (2008) Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J. Bacteriol. 190, 843-850
    • (2008) J. Bacteriol. , vol.190 , pp. 843-850
    • Li, F.1    Hinderberger, J.2    Seedorf, H.3    Zhang, J.4    Buckel, W.5    Thauer, R.K.6
  • 21
    • 38649143651 scopus 로고    scopus 로고
    • Energy conservation via electron-transferring flavoprotein in anaerobic bacteria
    • Herrmann, G., Jayamani, E., Mai, G., and Buckel, W. (2008) Energy conservation via electron-transferring flavoprotein in anaerobic bacteria. J. Bacteriol. 190, 784-791
    • (2008) J. Bacteriol. , vol.190 , pp. 784-791
    • Herrmann, G.1    Jayamani, E.2    Mai, G.3    Buckel, W.4
  • 22
    • 79952588675 scopus 로고    scopus 로고
    • Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
    • Kaster, A. K., Moll, J., Parey, K., and Thauer, R. K. (2011) Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl. Acad. Sci. U.S.A. 108, 2981-2986
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2981-2986
    • Kaster, A.K.1    Moll, J.2    Parey, K.3    Thauer, R.K.4
  • 23
    • 77957326597 scopus 로고    scopus 로고
    • + reduction with NADH are coupled via an electron bifurcating enzyme complex in Clostridium kluyveri
    • + reduction with NADH are coupled via an electron bifurcating enzyme complex in Clostridium kluyveri. J. Bacteriol. 192, 5115-5123
    • (2010) J. Bacteriol. , vol.192 , pp. 5115-5123
    • Wang, S.1    Huang, H.2    Moll, J.3    Thauer, R.K.4
  • 24
    • 0026553733 scopus 로고
    • Presence of a sodium-translocating ATPase in membrane vesicles of the homoacetogenic bacterium Acetobacterium woodii
    • Heise, R., Müller, V., and Gottschalk, G. (1992) Presence of a sodium-translocating ATPase in membrane vesicles of the homoacetogenic bacterium Acetobacterium woodii. Eur. J. Biochem. 206, 553-557
    • (1992) Eur. J. Biochem. , vol.206 , pp. 553-557
    • Heise, R.1    Müller, V.2    Gottschalk, G.3
  • 25
    • 0024430852 scopus 로고
    • Sodium dependence of acetate formation by the acetogenic bacterium Acetobacterium woodii
    • Heise, R., Müller, V., and Gottschalk, G. (1989) Sodium dependence of acetate formation by the acetogenic bacterium Acetobacterium woodii. J. Bacteriol. 171, 5473-5478
    • (1989) J. Bacteriol. , vol.171 , pp. 5473-5478
    • Heise, R.1    Müller, V.2    Gottschalk, G.3
  • 26
    • 0015464618 scopus 로고
    • Commentary on the Hungate technique for culture of anaerobic bacteria
    • Bryant, M. P. (1972) Commentary on the Hungate technique for culture of anaerobic bacteria. Am. J. Clin. Nutr. 25, 1324-1328
    • (1972) Am. J. Clin. Nutr. , vol.25 , pp. 1324-1328
    • Bryant, M.P.1
  • 27
    • 77956868541 scopus 로고
    • Norris, J. R., and Ribbons, D. W., eds Academic Press, New York
    • Hungate, R. E. (1969) in Methods in Microbiology (Norris, J. R., and Ribbons, D. W., eds) pp. 117-132, Academic Press, New York
    • (1969) Methods in Microbiology , pp. 117-132
    • Hungate, R.E.1
  • 28
    • 0017888541 scopus 로고
    • Arapid procedure for the purification of ferredoxin from clostridia using polyethylenimine
    • Schönheit, P., Wäscher, C., and Thauer, R. K. (1978)Arapid procedure for the purification of ferredoxin from clostridia using polyethylenimine. FEBS Lett. 89, 219-222
    • (1978) FEBS Lett. , vol.89 , pp. 219-222
    • Schönheit, P.1    Wäscher, C.2    Thauer, R.K.3
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification 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
  • 30
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish, W. W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 158, 357-364
    • (1988) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 31
    • 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
  • 32
    • 84555179630 scopus 로고    scopus 로고
    • Redox bifurcations. Mechanisms and importance to life now, and at its origin: A widespread means of energy conversion in biology unfolds
    • Nitschke, W., and Russell, M. J. (2012) Redox bifurcations. Mechanisms and importance to life now, and at its origin: a widespread means of energy conversion in biology unfolds. Bioessays 34, 106-109
    • (2012) Bioessays , vol.34 , pp. 106-109
    • Nitschke, W.1    Russell, M.J.2
  • 33
    • 0032799575 scopus 로고    scopus 로고
    • The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: Amino acid sequence analyses versus biochemical characterization
    • Verhagen, M. F., O'Rourke, T., and Adams, M. W. (1999) The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Biochim. Biophys. Acta 1412, 212-229
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 212-229
    • Verhagen, M.F.1    O'Rourke, T.2    Adams, M.W.3
  • 34
    • 67649413347 scopus 로고    scopus 로고
    • The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: A new perspective on anaerobic hydrogen production
    • Schut, G. J., and Adams, M. W. (2009) The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J. Bacteriol. 191, 4451-4457
    • (2009) J. Bacteriol. , vol.191 , pp. 4451-4457
    • Schut, G.J.1    Adams, M.W.2
  • 35
    • 84864008626 scopus 로고    scopus 로고
    • Electron bifurcation involved in the energy metabolism of the acetogenic bacterium Moorella thermoacetica growing on glucose or H2 plus CO2
    • Huang, H., Wang, S., Moll, J., and Thauer, R. K. (2012) Electron bifurcation involved in the energy metabolism of the acetogenic bacterium Moorella thermoacetica growing on glucose or H2 plus CO2. J. Bacteriol. 194, 3689-3699
    • (2012) J. Bacteriol. , vol.194 , pp. 3689-3699
    • Huang, H.1    Wang, S.2    Moll, J.3    Thauer, R.K.4
  • 36
    • 0017886452 scopus 로고
    • 2from equilibrium reactions with flavodoxins, methylviologen, and hydrogen plus hydrogenase
    • 2 from equilibrium reactions with flavodoxins, methylviologen, and hydrogen plus hydrogenase. Eur. J. Biochem. 85, 535-547
    • (1978) Eur. J. Biochem. , vol.85 , pp. 535-547
    • Mayhew, S.G.1
  • 37
    • 4344700076 scopus 로고    scopus 로고
    • A multisubunit membrane-bound [NiFe]-hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis
    • Soboh, B., Linder, D., and Hedderich, R. (2004) A multisubunit membrane-bound [NiFe]-hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis. Microbiology 150, 2451-2463
    • (2004) Microbiology , vol.150 , pp. 2451-2463
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 38
    • 77953200590 scopus 로고    scopus 로고
    • The surprising diversity of clostridial hydrogenases: A comparative genomic perspective
    • Calusinska, M., Happe, T., Joris, B., and Wilmotte, A. (2010) The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiology 156, 1575-1588
    • (2010) Microbiology , vol.156 , pp. 1575-1588
    • Calusinska, M.1    Happe, T.2    Joris, B.3    Wilmotte, A.4


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