Abstract:
: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 mumol.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 H2/CO2 grown Methanobacterium thermoautotrophicum (strain Marburg) is a molybdoenzyme.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Karrasch M,Börner G,Enssle M,Thauer RKdoi
10.1016/0014-5793(89)80964-0subject
Has Abstractpub_date
1989-08-14 00:00:00pages
226-30issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(89)80964-0journal_volume
253pub_type
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