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FAD requirement for the reduction of coenzyme F420 by formate dehydrogenase from Methanobacterium formicicum
- Source :
- Journal of Bacteriology; August 1983, Vol. 155 Issue: 2 p467-472, 6p
- Publication Year :
- 1983
-
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.
Details
- Language :
- English
- ISSN :
- 00219193 and 10985530
- Volume :
- 155
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- Journal of Bacteriology
- Publication Type :
- Periodical
- Accession number :
- ejs57603321
- Full Text :
- https://doi.org/10.1128/jb.155.2.467-472.1983