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pubmed-article:1633810pubmed:abstractTextMethanobacterium wolfei is a thermophilic methanogenic archaeon which requires tungsten or molybdenum for growth. We have found that the organism contains two formylmethanofuran dehydrogenases, one of which is a tungsten enzyme. Indirect evidence indicates that the other formylmethanofuran dehydrogenase is a molybdenum enzyme. The tungsten enzyme was purified and characterized. The native enzyme had an apparent molecular mass of 130 kDa. SDS/PAGE revealed a composition of three subunits of apparent molecular mass 35, 51 and 64 kDa, the N-terminal amino acid sequences of two of which were determined. 0.3-0.4 mol tungsten/mol enzyme was found but no molybdenum. The pterin cofactor was identified as molybdopterin guanine dinucleotide. The purified enzyme exhibited a specific activity of 8.3 mumol.min-1.mg protein-1 and an apparent Km for formylmethanofuran and methylviologen of 13 microM and 0.4 mM, respectively. The optimum temperature for activity was 65 degrees C. At 40-60 degrees C, the rate increased with a Q10 of 1.9; the activation energy of the reaction was 45 kJ/mol. The enzyme was found to require potassium ions for thermostability. The oxygen-sensitive enzyme was not inactivated by cyanide.lld:pubmed
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pubmed-article:1633810pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:1633810pubmed:articleTitleA tungsten-containing active formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei.lld:pubmed
pubmed-article:1633810pubmed:affiliationLaboratorium für Mikrobiologie, Philipps-Universität Marburg, Federal Republic of Germany.lld:pubmed
pubmed-article:1633810pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1633810pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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