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 language | English (US) |
|---|---|
| Pages (from-to) | 467-472 |
| Number of pages | 6 |
| Journal | Journal of bacteriology |
| Volume | 155 |
| Issue number | 2 |
| State | Published - Aug 1 1983 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Molecular Biology