FAD requirement for the reduction of coenzyme F420 by formate dehydrogenase from Methanobacterium formicicum.
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.
D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D019605:Euryarchaeota / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D005560:Formate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D010269:Paraquat / Q000378:metabolism; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000378:metabolism
D005182:Flavin-Adenine Dinucleotide; C015084:coenzyme F420; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D010269:Paraquat; D012256:Riboflavin