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Volumn 242, Issue 1, 1996, Pages 156-162

The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation

Author keywords

Iron sulfur proteins; Methanogenic Archaea; Molybdenum enzyme; Molybdopterin; Transcriptional regulation; Tungsten enzyme

Indexed keywords

MOLYBDENUM; OXIDOREDUCTASE; TUNGSTEN;

EID: 0029989411     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0156r.x     Document Type: Article
Times cited : (47)

References (30)
  • 2
    • 0028265243 scopus 로고
    • Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase
    • Bertram, P. A., Schmitz, R. A., Linder, D. & Thauer, R. K. (1994a) Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase, Arch. Microbiol. 161, 220-228.
    • (1994) Arch. Microbiol. , vol.161 , pp. 220-228
    • Bertram, P.A.1    Schmitz, R.A.2    Linder, D.3    Thauer, R.K.4
  • 3
    • 0028293448 scopus 로고
    • Formylmethanofuran dehydrogenases from methanogenic Archaea, Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulphur proteins
    • Bertram, P. A., Karrasch, M., Schmitz, R. A., Böcher, R., Albracht, S. P. J. & Thauer, R. K. (1994b) Formylmethanofuran dehydrogenases from methanogenic Archaea, Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulphur proteins, Eur. J. Biochem. 220, 477-484.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 477-484
    • Bertram, P.A.1    Karrasch, M.2    Schmitz, R.A.3    Böcher, R.4    Albracht, S.P.J.5    Thauer, R.K.6
  • 4
    • 0028596486 scopus 로고
    • Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum
    • Bertram, P. A. & Thauer, R. K. (1994) Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum, Eur. J. Biochem. 226, 811-818.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 811-818
    • Bertram, P.A.1    Thauer, R.K.2
  • 5
    • 0023954004 scopus 로고
    • Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum
    • Bokranz, M., Bäumner, G., Allmansberger, R., Ankel-Fuchs, D. & Klein, A. (1988) Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum, J. Bacteriol. 170, 568-577.
    • (1988) J. Bacteriol. , vol.170 , pp. 568-577
    • Bokranz, M.1    Bäumner, G.2    Allmansberger, R.3    Ankel-Fuchs, D.4    Klein, A.5
  • 6
    • 0025866022 scopus 로고
    • Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)
    • Börner, G., Karrasch, M. & Thauer, R. K. (1991) Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg), FEBS Lett. 290, 31-34.
    • (1991) FEBS Lett. , vol.290 , pp. 31-34
    • Börner, G.1    Karrasch, M.2    Thauer, R.K.3
  • 7
    • 0024850365 scopus 로고
    • Primer extension analysis of RNA
    • Boorstein, W. R. & Craig, E. A. (1989) Primer extension analysis of RNA, Methods Enzymol. 180, 247-369.
    • (1989) Methods Enzymol. , vol.180 , pp. 247-369
    • Boorstein, W.R.1    Craig, E.A.2
  • 8
    • 0024530633 scopus 로고
    • Gene structure, organization, and expression in archaebacteria
    • Brown, J. W., Daniels, C. J. & Reeve, J. N. (1989) Gene structure, organization, and expression in archaebacteria, Crit. Rev. Microbiol. 16, 287-338.
    • (1989) Crit. Rev. Microbiol. , vol.16 , pp. 287-338
    • Brown, J.W.1    Daniels, C.J.2    Reeve, J.N.3
  • 9
    • 0028961901 scopus 로고
    • Structure of a hyperthermopilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M. K., Mukund, S., Kletzin, A., Adams, M. W. W. & Rees, D. C. (1995) Structure of a hyperthermopilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267, 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 10
    • 0003108182 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix
    • Eckerskorn, C. & Lottspeich, F. (1989) Internal amino acid sequence analysis of proteins separated by gel electrophoresis after tryptic digestion in polyacrylamide matrix, Chromatographia 28, 92-94.
    • (1989) Chromatographia , vol.28 , pp. 92-94
    • Eckerskorn, C.1    Lottspeich, F.2
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids, J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. (1992) ABC transporters: from microorganisms to man, Annu. Rev. Cell. Biol. 8, 67-113.
    • (1992) Annu. Rev. Cell. Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 13
    • 0029583885 scopus 로고
    • The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide
    • Hochheimer, A., Schmitz, R. A., Thauer, R. K. & Hedderich, R. (1995) The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide, Eur. J. Biochem. 234, 910-920.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 910-920
    • Hochheimer, A.1    Schmitz, R.A.2    Thauer, R.K.3    Hedderich, R.4
  • 15
    • 0023131532 scopus 로고
    • Purification and use of Methanobacterium wolfei pseudomurein endopeptidase for lysis of Methanobacterium thermoautotrophicum
    • Kiener, A., König, H., Winter, J. & Leisinger, T. (1987) Purification and use of Methanobacterium wolfei pseudomurein endopeptidase for lysis of Methanobacterium thermoautotrophicum, J. Bacteriol. 169, 1010-1016.
    • (1987) J. Bacteriol. , vol.169 , pp. 1010-1016
    • Kiener, A.1    König, H.2    Winter, J.3    Leisinger, T.4
  • 16
    • 0029881337 scopus 로고
    • Organization and regulation of genes encoding the molybdenum nitrogenase and the alternative nitrogenase in Rhodobacter capsulatus
    • Masepohl, B. & Klipp, W. (1995) Organization and regulation of genes encoding the molybdenum nitrogenase and the alternative nitrogenase in Rhodobacter capsulatus, Arch. Microbiol 165, 80-90.
    • (1995) Arch. Microbiol , vol.165 , pp. 80-90
    • Masepohl, B.1    Klipp, W.2
  • 17
    • 0028908091 scopus 로고
    • In vivo definition of an archaeal promoter
    • Palmer, J. P. & Daniels, J. D. (1995) In vivo definition of an archaeal promoter, J. Bacteriol. 177, 1844-1849.
    • (1995) J. Bacteriol. , vol.177 , pp. 1844-1849
    • Palmer, J.P.1    Daniels, J.D.2
  • 18
    • 0026732105 scopus 로고
    • Molecular biology of methanogens
    • Reeve, J. N. (1992) Molecular biology of methanogens, Annu. Rev. Microbiol. 46, 165-191.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 165-191
    • Reeve, J.N.1
  • 23
    • 0030006891 scopus 로고    scopus 로고
    • Crystal strucure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopolan, K. V. & Rees, D. C. (1996) Crystal strucure of DMSO reductase: redox-linked changes in molybdopterin coordination, Science 272, 1615-1621.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopolan, K.V.4    Rees, D.C.5
  • 24
    • 0028227462 scopus 로고
    • Tungstate does not support synthesis of active formylmethanofuran dehydrogenase in Methanosarcina barkeri
    • Schmitz, R. A., Bertram, P. A. & Thauer, R. K. (1994) Tungstate does not support synthesis of active formylmethanofuran dehydrogenase in Methanosarcina barkeri, Arch. Microbiol. 161, 528-530.
    • (1994) Arch. Microbiol. , vol.161 , pp. 528-530
    • Schmitz, R.A.1    Bertram, P.A.2    Thauer, R.K.3
  • 26
    • 0021094214 scopus 로고
    • Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12
    • Stephens, P. E., Lewis, H. M., Darlison, M. G. & Guest, J. R. (1983) Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12, Eur. J. Biochem. 135, 519-527.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 519-527
    • Stephens, P.E.1    Lewis, H.M.2    Darlison, M.G.3    Guest, J.R.4
  • 27
    • 0028982893 scopus 로고
    • 10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg. Cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli
    • 10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg. Cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli, Eur. J. Biochem. 231, 773-778.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 773-778
    • Vaupel, M.1    Thauer, R.K.2
  • 28
    • 0028902975 scopus 로고
    • 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
    • 2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus, Arch Microbiol. 163, 112-118.
    • (1995) Arch Microbiol. , vol.163 , pp. 112-118
    • Vorholt, J.1    Kunow, J.2    Stetter, K.O.3    Thauer, R.K.4
  • 29
    • 0029915852 scopus 로고    scopus 로고
    • A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri
    • Vorholt, J., Vaupel, M. & Thauer, R. K. (1996) A polyferredoxin with eight [4Fe-4S] clusters as a 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.1    Vaupel, M.2    Thauer, R.K.3
  • 30
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A. & Bray, R. C. (1991) Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains, Biochim. Biophys. Acta 1057, 157-185.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.