Premium
Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme
Author(s) -
Karrasch M.,
Börner G.,
Enßle M.,
Thauer R.K.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80964-0
Subject(s) - methanosarcina barkeri , carbon monoxide dehydrogenase , enzyme , methanogenesis , biochemistry , methanobacterium , dehydrogenase , chemistry , formate dehydrogenase , methanosarcina , bacteria , biology , archaea , cofactor , catalysis , gene , genetics , carbon monoxide
Formylmethanofuran dehydrogenase, a key enzyme of methanogenesis, was purified 100‐fold from methanol grown Methanosarcina barkeri to apparent homogeneity and a specific activity of 34 μmol·min −1 ·mg protein −1 . Molybdenum was found to co‐migrate with the enzyme activity. The molybdenum content of purified preparations was 3–4 nmol per mg protein equal to 0.6–0.8 mol molybdenum per mol enzyme of apparent molecular mass 200 kDa. Evidence is presented that also formylmethanofuran dehydrogenase from H 2 /CO 2 grown Methanobacterium thermoautotrophicum (strain Marburg) is a molybdoenzyme.