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Volumn 192, Issue 3, 2010, Pages 674-678

Function of Ech hydrogenase in ferredoxin-dependent, membrane-bound electron transport in Methanosarcina mazei

Author keywords

[No Author keywords available]

Indexed keywords

ECH HYDROGENASE; FERREDOXIN; HYDROGENASE; UNCLASSIFIED DRUG;

EID: 75149154830     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01307-09     Document Type: Article
Times cited : (43)

References (28)
  • 1
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and the function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1
    • Abken, H. J., M. Tietze, J. Brodersen, S. Bäumer, U. Beifuss, and U. Deppenmeier. 1998. Isolation and characterization of methanophenazine and the function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180:2027-2032.
    • (1998) J. Bacteriol , vol.180 , pp. 2027-2032
    • Abken, H.J.1    Tietze, M.2    Brodersen, J.3    Bäumer, S.4    Beifuss, U.5    Deppenmeier, U.6
  • 2
    • 0034674063 scopus 로고    scopus 로고
    • The F420H2 dehydrogenase from Methanosarcina mazei is a redox-driven proton pump closely related to NADH dehydrogenases
    • Bäumer, S., T. Ide, C. Jacobi, A. Johann, G. Gottschalk, and U. Deppenmeier. 2000. The F420H2 dehydrogenase from Methanosarcina mazei is a redox-driven proton pump closely related to NADH dehydrogenases. J. Biol. Chem. 275:17968-17973.
    • (2000) J. Biol. Chem , vol.275 , pp. 17968-17973
    • Bäumer, S.1    Ide, T.2    Jacobi, C.3    Johann, A.4    Gottschalk, G.5    Deppenmeier, U.6
  • 3
    • 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
  • 4
    • 0033002713 scopus 로고    scopus 로고
    • Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus voltae
    • Brodersen, J., G. Gottschalk, and U. Deppenmeier. 1999. Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus voltae. Arch. Microbiol. 171:115-121.
    • (1999) Arch. Microbiol , vol.171 , pp. 115-121
    • Brodersen, J.1    Gottschalk, G.2    Deppenmeier, U.3
  • 6
    • 44449149379 scopus 로고    scopus 로고
    • Life close to the thermodynamic limit: How methanogenic archaea conserve energy
    • Deppenmeier, U., and V. Müller. 2008. Life close to the thermodynamic limit: how methanogenic archaea conserve energy. Results Probl. Cell Differ. 45:123-152.
    • (2008) Results Probl. Cell Differ , vol.45 , pp. 123-152
    • Deppenmeier, U.1    Müller, V.2
  • 7
  • 8
    • 0347622759 scopus 로고    scopus 로고
    • Flavin mononucleotide-binding flavoprotein family in the domain Archaea
    • Ding, Y. H., and J. G. Ferry. 2004. Flavin mononucleotide-binding flavoprotein family in the domain Archaea. J. Bacteriol. 186:90-97.
    • (2004) J. Bacteriol , vol.186 , pp. 90-97
    • Ding, Y.H.1    Ferry, J.G.2
  • 9
    • 0023658408 scopus 로고
    • On the role of N-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane
    • Ellermann, J., A. Kobelt, A. Pfaltz, and R. K. Thauer. 1987. On the role of N-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane. FEBS Lett. 220:358-362.
    • (1987) FEBS Lett , vol.220 , pp. 358-362
    • Ellermann, J.1    Kobelt, A.2    Pfaltz, A.3    Thauer, R.K.4
  • 10
    • 41349089084 scopus 로고    scopus 로고
    • Methanogenesis in marine sediments
    • Ferry, J. G., and D. J. Lessner. 2008. Methanogenesis in marine sediments. Ann. N. Y. Acad. Sci. 1125:147-157.
    • (2008) Ann. N. Y. Acad. Sci , vol.1125 , pp. 147-157
    • Ferry, J.G.1    Lessner, D.J.2
  • 11
    • 0036225678 scopus 로고    scopus 로고
    • The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity
    • Galagan, J. E., et al. 2002. The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity. Genome Res. 12:532-542.
    • (2002) Genome Res , vol.12 , pp. 532-542
    • Galagan, J.E.1
  • 12
    • 0345194051 scopus 로고
    • Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri
    • Hippe, H., D. Caspari, K. Fiebig, and G. Gottschalk. 1979. Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri. Proc. Natl. Acad. Sci. U. S. A. 76:494-498.
    • (1979) Proc. Natl. Acad. Sci. U. S. A , vol.76 , pp. 494-498
    • Hippe, H.1    Caspari, D.2    Fiebig, K.3    Gottschalk, G.4
  • 14
    • 0032586857 scopus 로고    scopus 로고
    • Energy conservation by the H2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: Identification of two proton-translocating segments
    • Ide, T., S. Bäumer, and U. Deppenmeier. 1999. Energy conservation by the H2:heterodisulfide oxidoreductase from Methanosarcina mazei Gö1: identification of two proton-translocating segments. J. Bacteriol. 181:4076-4080.
    • (1999) J. Bacteriol , vol.181 , pp. 4076-4080
    • Ide, T.1    Bäumer, S.2    Deppenmeier, U.3
  • 15
    • 67749124076 scopus 로고    scopus 로고
    • Transcriptional profiling of methyltransferase genes during growth of Methanosarcina mazei on trimethylamine
    • Krätzer, C., P. Carini, R. Hovey, and U. Deppenmeier. 2009. Transcriptional profiling of methyltransferase genes during growth of Methanosarcina mazei on trimethylamine. J. Bacteriol. 191:5108-5115.
    • (2009) J. Bacteriol , vol.191 , pp. 5108-5115
    • Krätzer, C.1    Carini, P.2    Hovey, R.3    Deppenmeier, U.4
  • 16
    • 35048877274 scopus 로고    scopus 로고
    • The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster
    • Lessner, D. J., and J. G. Ferry. 2007. The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster. J. Bacteriol. 189:7475-7484.
    • (2007) J. Bacteriol , vol.189 , pp. 7475-7484
    • Lessner, D.J.1    Ferry, J.G.2
  • 17
    • 33847369414 scopus 로고    scopus 로고
    • Quantitative proteomic and microarray analysis of the archaeon Methanosarcina acetivorans grown with acetate versus methanol
    • Li, L., Q. Li, L. Rohlin, U. Kim, K. Salmon, T. Rejtar, R. P. Gunsalus, B. L. Karger, and J. G. Ferry. 2007. Quantitative proteomic and microarray analysis of the archaeon Methanosarcina acetivorans grown with acetate versus methanol. J. Proteome Res. 6:759-771.
    • (2007) J. Proteome Res , vol.6 , pp. 759-771
    • Li, L.1    Li, Q.2    Rohlin, L.3    Kim, U.4    Salmon, K.5    Rejtar, T.6    Gunsalus, R.P.7    Karger, B.L.8    Ferry, J.G.9
  • 19
    • 0030900723 scopus 로고    scopus 로고
    • A genetic system for Archaea of the genus Methanosarcina: Liposomemediated transformation and construction of shuttle vectors
    • Metcalf, W. W., J. K. Zhang, E. Apolinario, K. R. Sowers, and R. S. Wolfe. 1997. A genetic system for Archaea of the genus Methanosarcina: liposomemediated transformation and construction of shuttle vectors. Proc. Natl. Acad. Sci. U. S. A. 94:2626-2631.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 2626-2631
    • Metcalf, W.W.1    Zhang, J.K.2    Apolinario, E.3    Sowers, K.R.4    Wolfe, R.S.5
  • 20
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., S. Bartoschek, J. Koch, A. Künkel, 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    Künkel, A.4    Hedderich, R.5
  • 21
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer, J., H. C. Kuettner, J. K. Zhang, R. Hedderich, and W. W. Metcalf. 2002. Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl. Acad. Sci. U. S. A. 99:5632-5637.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 22
    • 4243811585 scopus 로고
    • Purification and analysis of ferredoxin from Clostridium pasteurianum
    • Mortenson, L. E. 1964. Purification and analysis of ferredoxin from Clostridium pasteurianum. Biochim. Biophys. Acta 81:71-77.
    • (1964) Biochim. Biophys. Acta , vol.81 , pp. 71-77
    • Mortenson, L.E.1
  • 23
    • 0006250620 scopus 로고
    • Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum
    • Noll, K. M., K. L. Rinehart, Jr., R. S. Tanner, and R. S. Wolfe. 1986. Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum. Proc. Natl. Acad. Sci. U. S. A. 83:4238-4242.
    • (1986) Proc. Natl. Acad. Sci. U. S. A , vol.83 , pp. 4238-4242
    • Noll, K.M.1    Rinehart Jr., K.L.2    Tanner, R.S.3    Wolfe, R.S.4
  • 24
    • 0028130513 scopus 로고
    • Characterization of a CO:heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila
    • Peer, C. W., M. H. Painter, M. E. Rasche, and J. G. Ferry. 1994. Characterization of a CO:heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila. J. Bacteriol. 176:6974-6979.
    • (1994) J. Bacteriol , vol.176 , pp. 6974-6979
    • Peer, C.W.1    Painter, M.H.2    Rasche, M.E.3    Ferry, J.G.4
  • 25
    • 0021079728 scopus 로고
    • Isolation of carbon monoxide dehydrogenase from Acetobacterium woodii and comparison of its properties with those of the Clostridium thermoaceticum enzyme
    • Ragsdale, S. W., L. G. Ljungdahl, and D. V. Der Vartanian. 1983. Isolation of carbon monoxide dehydrogenase from Acetobacterium woodii and comparison of its properties with those of the Clostridium thermoaceticum enzyme. J. Bacteriol. 155:1224-1237.
    • (1983) J. Bacteriol , vol.155 , pp. 1224-1237
    • Ragsdale, S.W.1    Ljungdahl, L.G.2    Der Vartanian, D.V.3
  • 27
    • 47549119041 scopus 로고    scopus 로고
    • Methanogenic archaea: Ecologically relevant differences in energy conservation
    • Thauer, R. K., A. K. Kaster, H. Seedorf, W. Buckel, and R. Hedderich. 2008. Methanogenic archaea: ecologically relevant differences in energy conservation. Nat. Rev. Microbiol. 6:579-591.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 579-591
    • Thauer, R.K.1    Kaster, A.K.2    Seedorf, H.3    Buckel, W.4    Hedderich, R.5
  • 28
    • 0014429125 scopus 로고
    • A specific and sensitive assay for disulfides
    • Zahler, W. L., and W. W. Cleland. 1968. A specific and sensitive assay for disulfides. J. Biol. Chem. 243:716-719.
    • (1968) J. Biol. Chem , vol.243 , pp. 716-719
    • Zahler, W.L.1    Cleland, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.