Methanobacterium wolfei

Winter J, C Lerp, H-P Zabel, F X Wildenaner, H Konig, F Schindler (1984) Methanobacterium wolfei, sp. nov., a new tungsten-requiring, thermophilic, autotrophic methanogen. Syst Appl Microbiol 5 457-466. 

EPR spectrum, 32 323, 325 EXAFS studies, 32 309 Methanobacterium wolfei, formyl methanofuran dehydrogenase, 40 73... 

Schmitz, R. A., Albracht, S. P. J., and Thauer, R. K., 1992, A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei, Eur. J. Biochem. 209 1013nl018. 

The growth of Methanobacterium wolfei is dependent on the presence of molybdenum or tungsten, and one of the two formylmethanofuran dehydrogenases from this bacterium is a tungsten enzyme (285). The reversible reaction catalyzed by these enzymes (Eq. (29)) is the first step in methane formation from CO2 in all methanogenic Archaea (286). 

It is present (with varying specific activities) in H2—C02-grown M. thermoautotrophicum, Methanobacterium wolfei, and Methanobrevibacter arboriphilus, H2-... 

There are much fewer EPR studies on W- than on Mo-enzymes since there is only a small number of known W-enzymes. With the exception of the W-substituted Rat liver SO and of Methanobacterium wolfei Formylmethano-furan dehydrogenase (FMDH), to our knowledge all EPR-characterized W-enzymes have a bisPPT cofactor. 

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