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Volumn 165, Issue 3, 1996, Pages 187-193

Purification, properties and primary structure of H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus

Author keywords

Archaea; H2 Forming dehydrogenase; Hydrogenases; Methane formation; Methanococcus; N5,N10 Methylenetetrahydromethanopterin

Indexed keywords

HYDROGENASE; RIBOSOME RNA;

EID: 0029869181     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf01692860     Document Type: Article
Times cited : (35)

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
    • 0003383552 scopus 로고
    • 2 ohne Metall und ihre Analogie zur Chemie der Alkane in supersaurer Lösung
    • 2 ohne Metall und ihre Analogie zur Chemie der Alkane in supersaurer Lösung. Angew Chem 107: 2418-2421
    • (1995) Angew Chem , vol.107 , pp. 2418-2421
    • Berkessel, A.1    Thauer, R.K.2
  • 3
    • 1542602052 scopus 로고
    • Bio-Rad Laboratories, Richmond, Calif., USA
    • Bio-Rad Laboratories (1990) Instruction manual for Bio-Rad Protein assay. Bio-Rad Laboratories, Richmond, Calif., USA
    • (1990) Instruction Manual for Bio-Rad Protein Assay
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the prinziple of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the prinziple of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0027076754 scopus 로고
    • Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri
    • Breitung J, Börner G, Scholz S, Linder D, Stetter KO, Thauer RK (1992) Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri. Eur J Biochem 210: 971-981
    • (1992) Eur J Biochem , vol.210 , pp. 971-981
    • Breitung, J.1    Börner, G.2    Scholz, S.3    Linder, D.4    Stetter, K.O.5    Thauer, R.K.6
  • 7
    • 13144267947 scopus 로고
    • The cyanogen bromide reaction
    • Gross E (1967) The cyanogen bromide reaction. Methods Enzymol 11:238-253
    • (1967) Methods Enzymol , vol.11 , pp. 238-253
    • Gross, E.1
  • 8
    • 0019900712 scopus 로고
    • Methanococcus thermolithotrophicus, a novel thermophilic lithotrophic methanogen
    • Huber H, Thomm M, König H, Thies G, Stetter KO (1982) Methanococcus thermolithotrophicus, a novel thermophilic lithotrophic methanogen. Arch Microbiol 132:47-50
    • (1982) Arch Microbiol , vol.132 , pp. 47-50
    • Huber, H.1    Thomm, M.2    König, H.3    Thies, G.4    Stetter, K.O.5
  • 10
    • 0028832444 scopus 로고
    • 10-methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea
    • 10-methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea. Eur J Biochem 233:372-376
    • (1995) Eur J Biochem , vol.233 , pp. 372-376
    • Klein, A.R.1    Hartmann, G.C.2    Thauer, R.K.3
  • 12
    • 0027296127 scopus 로고
    • Phylogenetic analysis of thermophilic Methanobacterium sp.: Evidence for a formate-utilizing ancestor
    • Nölling J, Hahn D, Ludwig W, De Vos WM (1993) Phylogenetic analysis of thermophilic Methanobacterium sp.: evidence for a formate-utilizing ancestor. System Appl Microbiol 16:208-215
    • (1993) System Appl Microbiol , vol.16 , pp. 208-215
    • Nölling, J.1    Hahn, D.2    Ludwig, W.3    De Vos, W.M.4
  • 13
    • 0029066823 scopus 로고
    • Organization and growth phase-dependent transcription of methane genes in two regions of the Methanobacterium thermoautotrophicum genome
    • Nölling J, Pihl TD, Vriesema A, Reeve JN (1995) Organization and growth phase-dependent transcription of methane genes in two regions of the Methanobacterium thermoautotrophicum genome. J Bacteriol 177:2460-2468
    • (1995) J Bacteriol , vol.177 , pp. 2460-2468
    • Nölling, J.1    Pihl, T.D.2    Vriesema, A.3    Reeve, J.N.4
  • 14
    • 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
  • 18
    • 0028179135 scopus 로고
    • 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional NMR spectroscopy
    • 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional NMR spectroscopy. Biochemistry 33:3986-3993
    • (1994) Biochemistry , vol.33 , pp. 3986-3993
    • Schleucher, J.1    Griesinger, C.2    Schwörer, B.3    Thauer, R.K.4
  • 19
    • 0001250303 scopus 로고
    • Elucidation of the stereochemical course of chemical reactions by magnetic labeling
    • Schleucher J, Schwörer B, Thauer RK, Griesinger C (1995) Elucidation of the stereochemical course of chemical reactions by magnetic labeling. J Am Chem Soc 117:2941-2942
    • (1995) J Am Chem Soc , vol.117 , pp. 2941-2942
    • Schleucher, J.1    Schwörer, B.2    Thauer, R.K.3    Griesinger, C.4
  • 20
    • 0025877458 scopus 로고
    • Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic bacteria
    • Schwörer B, Thauer RK (1991) Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin 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
    • 0027016372 scopus 로고
    • In vivo excision properties of bacteriophage λ ZAP expression vectors
    • Short JM, Sorge JA (1992) In vivo excision properties of bacteriophage λ ZAP expression vectors. Methods Enzymol 216:495-508
    • (1992) Methods Enzymol , vol.216 , pp. 495-508
    • Short, J.M.1    Sorge, J.A.2
  • 23
    • 0026021816 scopus 로고
    • Physical and genetic map of the Methanococcus voltae chromosome
    • Sitzmann J, Klein A (1991) Physical and genetic map of the Methanococcus voltae chromosome. Mol Microbiol 5(2):505-513
    • (1991) Mol Microbiol , vol.5 , Issue.2 , pp. 505-513
    • Sitzmann, J.1    Klein, A.2
  • 24
    • 0024644241 scopus 로고
    • Primary structure, functional organization and expression of nitrogenase structural genes of the thermophilic archaebacterium Methanococcus thermolithotrophicus
    • Souillard N, Sibold L (1989) Primary structure, functional organization and expression of nitrogenase structural genes of the thermophilic archaebacterium Methanococcus thermolithotrophicus. Mol Microbiol 3:541-551
    • (1989) Mol Microbiol , vol.3 , pp. 541-551
    • Souillard, N.1    Sibold, L.2
  • 26
    • 0028207371 scopus 로고
    • Transcription factors and termination of transcription in Methanococcus
    • Thomm M, Hausner W, Hethke C (1994) Transcription factors and termination of transcription in Methanococcus. Syst Appl Microbiol 16:648-655
    • (1994) Syst Appl Microbiol , vol.16 , pp. 648-655
    • Thomm, M.1    Hausner, W.2    Hethke, C.3
  • 27
    • 0026338480 scopus 로고
    • 420-reducing methylene tetrahydrome-thanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum (Marburg)
    • 420-reducing methylene tetrahydrome-thanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum (Marburg). Eur J Biochem 202:1205-1208
    • (1991) Eur J Biochem , vol.202 , pp. 1205-1208
    • Von Bünau, R.1    Zirngibl, C.2    Thauer, R.K.3    Klein, A.4
  • 28
    • 0023432347 scopus 로고
    • Structure and organization of the hisA gene of the thermophilic archaebacterium Methanococcus thermolithotrophicus
    • Weil CF, Beckler GS, Reeve JN (1987) Structure and organization of the hisA gene of the thermophilic archaebacterium Methanococcus thermolithotrophicus. J Bacteriol 169:4857-4860
    • (1987) J Bacteriol , vol.169 , pp. 4857-4860
    • Weil, C.F.1    Beckler, G.S.2    Reeve, J.N.3
  • 29
    • 0025014263 scopus 로고
    • 10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity
    • 10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Letters 261:112-116
    • (1990) FEBS Letters , vol.261 , pp. 112-116
    • Zirngibl, C.1    Hedderich, R.2    Thauer, R.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.