FAD requirement for the reduction of coenzyme F420 by formate dehydrogenase from Methanobacterium formicicum.

N. L. Schauer, James Gregory Ferry

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

The partial purification of the formate dehydrogenase from cell-free extracts of Methanobacterium formicicum decreased the rate of coenzyme F420 reduction 175-fold relative to the rate of methyl viologen reduction. FAD, isolated from this organism, reactivated the coenzyme F420-dependent activity of purified formate dehydrogenase and restored the activity ratio (coenzyme F420/methyl viologen) to near that in cell-free extracts. Neither flavin mononucleotide nor FADH2 replaced FAD. The reduced form of FAD inhibited the reactivation of coenzyme F420-dependent formate dehydrogenase activity by the oxidized form. The results suggest that native formate dehydrogenase from Methanobacterium formicicum contains noncovalently bound FAD that is required for coenzyme F420-dependent activity.

Original languageEnglish (US)
Pages (from-to)467-472
Number of pages6
JournalJournal of bacteriology
Volume155
Issue number2
StatePublished - Aug 1 1983

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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