메뉴 건너뛰기




Volumn 71, Issue 6, 2005, Pages 2870-2874

Energy generation from the CO oxidation-hydrogen production pathway in Rubrivivax gelatinosus

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; ENERGY MANAGEMENT; GROWTH KINETICS; HYDROGEN; OXIDATION; REACTION KINETICS; STOICHIOMETRY; SYNTHESIS (CHEMICAL);

EID: 20444377225     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.6.2870-2874.2005     Document Type: Article
Times cited : (52)

References (26)
  • 1
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • Andrews, S. C., B. C. Berks, J. McClay, A. Ambler, M. A. Quail, P. Golby, and J. R. Guest. 1997. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143:3633-3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 2
    • 0014184404 scopus 로고
    • The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation
    • Beechey, R. B., A. M. Roberton, C. T. Holloway, and I. G. Knight. 1967. The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation. Biochemistry 6:3867-3879.
    • (1967) Biochemistry , vol.6 , pp. 3867-3879
    • Beechey, R.B.1    Roberton, A.M.2    Holloway, C.T.3    Knight, I.G.4
  • 3
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli encoding for formate hydrogenlyase components
    • Böhm, R., M. Sauter, and A. Böck. 1990. Nucleotide sequence and expression of an operon in Escherichia coli encoding for formate hydrogenlyase components. Mol. Microbiol. 4:231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 4
    • 0021222858 scopus 로고
    • Carbon monoxide dehydrogenase from Rhodospirillum rubrum
    • Bonam, D., A. A. Murrell, and P. W. Ludden. 1984. Carbon monoxide dehydrogenase from Rhodospirillum rubrum. J. Bacteriol. 159:693-699.
    • (1984) J. Bacteriol. , vol.159 , pp. 693-699
    • Bonam, D.1    Murrell, A.A.2    Ludden, P.W.3
  • 5
    • 0022779582 scopus 로고
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri. Eur. J. Biochem. 159:393-398.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 393-398
    • Bott, M.1    Elkmanns, B.2    Thauer, R.K.3
  • 6
    • 0008883773 scopus 로고
    • Regulation of anaerobic carbon monoxide oxidation activity in Rhodocyclus gelatinosus
    • Champine, J. E., and R. L. Uffen. 1987. Regulation of anaerobic carbon monoxide oxidation activity in Rhodocyclus gelatinosus. FEMS Microbiol. 44:307-311.
    • (1987) FEMS Microbiol. , vol.44 , pp. 307-311
    • Champine, J.E.1    Uffen, R.L.2
  • 8
    • 0025954526 scopus 로고
    • 2 evolution system of Rhodospirillum rubrum
    • 2 evolution system of Rhodospirillum rubrum. J. Biol. Chem. 27:18395-18403.
    • (1991) J. Biol. Chem. , vol.27 , pp. 18395-18403
    • Ensign, S.A.1    Ludden, P.W.2
  • 10
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J. D., Y. He, D. Shelver, G. P. Roberts, and P. W. Ludden. 1996. Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178:6200-6208.
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 11
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • Fox, J. D., R. L. Kerby, G. P. Roberts, and P. W. Ludden. 1996. Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178:1515-1524.
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1524
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 12
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich, T., and D. Scheide. 2000. The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479:1-5.
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 13
    • 0015359973 scopus 로고
    • Conservation and transformation of energy by bacterial membranes
    • Harold, F. M. 1972. Conservation and transformation of energy by bacterial membranes. Bacteriol. Rev. 36:172-230.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 172-230
    • Harold, F.M.1
  • 14
    • 0028925554 scopus 로고
    • Carbon monoxide-dependent growth of Rhodospirillum rubrum
    • Kerby, R. L., P. W. Ludden, and G. P. Roberts. 1995. Carbon monoxide-dependent growth of Rhodospirillum rubrum. J. Bacteriol. 177:2241-2244.
    • (1995) J. Bacteriol. , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 17
    • 0036275140 scopus 로고    scopus 로고
    • Characterization of the oxygen tolerance of a hydrogenase linked to a carbon monoxide oxidation pathway in Rubrivivax gelatinosus
    • Maness, P. C., S. Smolinski, A. C. Dillon, M. J. Heben, and P. F. Weaver. 2002. Characterization of the oxygen tolerance of a hydrogenase linked to a carbon monoxide oxidation pathway in Rubrivivax gelatinosus. Appl. Environ. Microbiol. 68:2633-2636.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2633-2636
    • Maness, P.C.1    Smolinski, S.2    Dillon, A.C.3    Heben, M.J.4    Weaver, P.F.5
  • 18
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • Mathiesen, C., and C. Hägerhäll. 2002. Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters. Biochim. Biophys. Acta 1556:121-132.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 121-132
    • Mathiesen, C.1    Hägerhäll, C.2
  • 19
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., S. Bartoschek, J. Koch, A. Kunkel, and R. Hedderich. 1999. Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 265:325-335.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Kunkel, A.4    Hedderich, R.5
  • 20
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: Proton reduction coupled to proton translocation
    • Sapra, R., K. Bagramyan, and M. W. W. Adams. 2003. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc. Natl. Acad. Sci. USA 100:7545-7550.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.W.3
  • 21
    • 0000249418 scopus 로고
    • Dicyclohexylcarbodiimide as a probe for proton translocating enzymes
    • Solioz, M. 1984. Dicyclohexylcarbodiimide as a probe for proton translocating enzymes. Trends Biochem. Sci. 9:309-312.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 309-312
    • Solioz, M.1
  • 22
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • Tersteegen, A., and R. Hedderich. 1999. Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur. J. Biochem. 264:930-943.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 23
    • 0032518432 scopus 로고    scopus 로고
    • Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation
    • Tran, Q. H., and G. Unden. 1998. Changes in the proton potential and the cellular energetics of Escherichia coli during growth by aerobic and anaerobic respiration or by fermentation. Eur. J. Biochem. 251:538-543.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 538-543
    • Tran, Q.H.1    Unden, G.2
  • 24
    • 1342293305 scopus 로고
    • Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate
    • Uffen, R. L. 1976. Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate. Proc. Natl. Acad. Sci. USA 73:3298-3302.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3298-3302
    • Uffen, R.L.1
  • 25
    • 0019584408 scopus 로고
    • Metabolism of carbon monoxide
    • Uffen, R. L. 1981. Metabolism of carbon monoxide. Enzyme Microbiol. Technol. 3:197-206.
    • (1981) Enzyme Microbiol. Technol. , vol.3 , pp. 197-206
    • Uffen, R.L.1
  • 26
    • 0020509698 scopus 로고
    • Metabolism of carbon monoxide by Rhodopseudomonas gelatinosa: Cell growth and properties of the oxidation system
    • Uffen, R. L. 1983. Metabolism of carbon monoxide by Rhodopseudomonas gelatinosa: cell growth and properties of the oxidation system. J. Bacteriol. 155:956-965.
    • (1983) J. Bacteriol. , vol.155 , pp. 956-965
    • Uffen, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.