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  • Methanobacterium  (1)
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    ISSN: 1432-072X
    Keywords: Tungsten enzymes ; Molybdenum enzymes ; Formylmethanofuran dehydrogenase ; Methanogenic Archaea ; Methanosarcina barkeri ; Methanobacterium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell extracts of Methanosarcina barkeri grown on methanol in media supplemented with molybdate exhibited a specific activity of formylmethanofuran dehydrogenase of approximately 1 U (1 μmol/min)/mg protein. When the growth medium was supplemented with tungstate rather than with molybdate, the specific activity was only 0.04 U/mg. Despite this reduction in specific activity growth on methanol was not inhibited. An inhibition of both growth and synthesis of active formylmethanofuran dehydrogenase was observed, however, when H2 and CO2 were the energy substrates. The results indicate that, in contrast to Methanobacterium wolfei and Methanobacterium thermoautotrophicum, M. barkeri possesses only a molybdenum containing formylmethanofuran dehydrogenase and not in addition a tungsten isoenzyme.
    Type of Medium: Electronic Resource
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