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Volumn 169, Issue 3, 1998, Pages 201-205

Two F420-reducing hydrogenases in Methanosarcina barkeri

Author keywords

Coenzyme F420; Gene expression; Hydrogenases; Methanogenic archaea; Methanosarcina barkeri

Indexed keywords

HYDROGENASE; METHANOL; TRIMETHYLAMINE;

EID: 0031908850     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050561     Document Type: Article
Times cited : (26)

References (30)
  • 1
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht SPJ (1994) Nickel hydrogenases: in search of the active site. Biochim Biophys Acta 1188:167-204
    • (1994) Biochim Biophys Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.J.1
  • 2
    • 0025333468 scopus 로고
    • Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum DH
    • Alex LA, Reeve JN, Orme-Johnson WH, Walsh CT (1990) Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum DH. Biochemistry 29:7237-7244
    • (1990) Biochemistry , vol.29 , pp. 7237-7244
    • Alex, L.A.1    Reeve, J.N.2    Orme-Johnson, W.H.3    Walsh, C.T.4
  • 5
    • 0024850365 scopus 로고
    • Primer extension analysis of RNA
    • Dahlberg JE, Abelson JN (eds) Academic Press, New York London
    • Boorstein WR, Craig EA (1989) Primer extension analysis of RNA. In: Dahlberg JE, Abelson JN (eds) Methods in enzymology, vol 180. Academic Press, New York London, pp 347-369
    • (1989) Methods in Enzymology , vol.180 , pp. 347-369
    • Boorstein, W.R.1    Craig, E.A.2
  • 7
    • 0028790975 scopus 로고
    • Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl
    • Deppenmeier U (1995) Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl. Arch Microbiol 164:370-376
    • (1995) Arch Microbiol , vol.164 , pp. 370-376
    • Deppenmeier, U.1
  • 8
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, both encoding a membrane-bound hydrogenase and a cytochrome b
    • Deppenmeier U, Blaut M, Lentes S, Herzberg C, Gottschalk G (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, both encoding a membrane-bound hydrogenase and a cytochrome b. Eur J Biochem 227: 261-269
    • (1995) Eur J Biochem , vol.227 , pp. 261-269
    • Deppenmeier, U.1    Blaut, M.2    Lentes, S.3    Herzberg, C.4    Gottschalk, G.5
  • 9
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • Deppenmeier U, Müller V, Gottschalk G (1996) Pathways of energy conservation in methanogenic archaea. Arch Microbiol 165:149-163
    • (1996) Arch Microbiol , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Müller, V.2    Gottschalk, G.3
  • 10
    • 0025797295 scopus 로고
    • 10-methylenetetrahydromethanopterin dehydrogenase in methanol-grown Methanosarcina barkeri
    • 10-methylenetetrahydromethanopterin dehydrogenase in methanol-grown Methanosarcina barkeri. Arch Microbiol 155:483-490
    • (1991) Arch Microbiol , vol.155 , pp. 483-490
    • Enßle, M.1    Zirngibl, C.2    Linder, D.3    Thauer, R.K.4
  • 11
    • 0024727930 scopus 로고
    • 420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)
    • 420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro). Eur J Biochem 184:79-88
    • (1989) Eur J Biochem , vol.184 , pp. 79-88
    • Fiebig, K.1    Friedrich, B.2
  • 14
    • 0029671414 scopus 로고    scopus 로고
    • Methylcobalamin: Coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri: cloning, sequencing and differential transcription of the encoding genes and functional overexpression of the mtaA gene in Escherichia coli
    • Harms U, Thauer RK (1996) Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri: cloning, sequencing and differential transcription of the encoding genes and functional overexpression of the mtaA gene in Escherichia coli. Eur J Biochem 235:653-659
    • (1996) Eur J Biochem , vol.235 , pp. 653-659
    • Harms, U.1    Thauer, R.K.2
  • 15
    • 0000549132 scopus 로고
    • Carbonic anhydrase activity in acetate-grown Methanosarcina barkeri
    • Karrasch M, Bott M, Thauer RK (1989) Carbonic anhydrase activity in acetate-grown Methanosarcina barkeri. Arch Microbiol 151:137-142
    • (1989) Arch Microbiol , vol.151 , pp. 137-142
    • Karrasch, M.1    Bott, M.2    Thauer, R.K.3
  • 16
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme
    • Künkel A, Vaupel M, Heim S, Thauer RK, Hedderich R (1997) Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme. Eur J Biochem 244:226-234
    • (1997) Eur J Biochem , vol.244 , pp. 226-234
    • Künkel, A.1    Vaupel, M.2    Heim, S.3    Thauer, R.K.4    Hedderich, R.5
  • 17
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 18
    • 0025376474 scopus 로고
    • Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to Blue Sepharose C1-6B
    • Ma K, Thauer RK (1990) Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to Blue Sepharose C1-6B. FEBS Lett 268:59-62
    • (1990) FEBS Lett , vol.268 , pp. 59-62
    • Ma, K.1    Thauer, R.K.2
  • 19
    • 0026732105 scopus 로고
    • Molecular biology of methanogens
    • Reeve JN (1992) Molecular biology of methanogens. Annu Rev Microbiol 46:165-191
    • (1992) Annu Rev Microbiol , vol.46 , pp. 165-191
    • Reeve, J.N.1
  • 21
    • 0025877458 scopus 로고
    • Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydro-methanopterin reductase, and heterodisulfide reductase in methanogenic bacteria
    • Schwörer B, Thauer RK (1991) Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydro-methanopterin reductase, and heterodisulfide reductase in methanogenic bacteria. Arch Microbiol 155:459-465
    • (1991) Arch Microbiol , vol.155 , pp. 459-465
    • Schwörer, B.1    Thauer, R.K.2
  • 22
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: Functional analysis and comparative genomics
    • Smith DR, Doucette-Stamm LA, Deloughery C, et al (1997) Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: functional analysis and comparative genomics. J Bacteriol 179:7135-7155
    • (1997) J Bacteriol , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3
  • 23
    • 0030957417 scopus 로고    scopus 로고
    • The [NiFe] hydrogenases of Methanococcus voltae: Genes, enzymes and regulation
    • Sorgenfrei O, Müller S, Pfeiffer M, Sniezko I, Klein A (1997) The [NiFe] hydrogenases of Methanococcus voltae: genes, enzymes and regulation. Arch Microbiol 167:189-195
    • (1997) Arch Microbiol , vol.167 , pp. 189-195
    • Sorgenfrei, O.1    Müller, S.2    Pfeiffer, M.3    Sniezko, I.4    Klein, A.5
  • 25
    • 0031029161 scopus 로고    scopus 로고
    • The biodiversity and unity in biochemistry
    • Thauer RK (1997) The biodiversity and unity in biochemistry. Antonie Van Leeuwenhoek 71:21-32
    • (1997) Antonie Van Leeuwenhoek , vol.71 , pp. 21-32
    • Thauer, R.K.1
  • 29
    • 0029915852 scopus 로고    scopus 로고
    • A polyferredoxin with eight [4Fe-4S] clusters as subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri
    • Vorholt JA, Vaupel M, Thauer RK (1996) A polyferredoxin with eight [4Fe-4S] clusters as subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri. Eur J Biochem 236:309-317
    • (1996) Eur J Biochem , vol.236 , pp. 309-317
    • Vorholt, J.A.1    Vaupel, M.2    Thauer, R.K.3
  • 30
    • 0027481498 scopus 로고
    • Methanogenesis and the unity of biochemistry
    • Weiss DS, Thauer RK (1993) Methanogenesis and the unity of biochemistry. Cell 72:819-822
    • (1993) Cell , vol.72 , pp. 819-822
    • Weiss, D.S.1    Thauer, R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.