NADH and NADPH-viologen reductases from Acinetobacter calcoaceticus.
Three pyridine nucleotide-dependent diaphorases have been isolated from Acinetobacter calcoaceticus cells and partially characterized. Two of them, with molecular weights of 165,000 and 57,000, utilize NADPH as electron donor whereas the third one (MW = 57,000) is specific for NADH. Oxidized viologen dyes, flavin nucleotides, dichlorophenol indophenol and ferricyanide can act with efficiency as acceptors in the reaction mediated by these diaphorases. The diaphorase activities have been characterized kinetically, and the effect of different inhibitors and cofactors has been also studied. The diaphorases seem to be subjected to metabolic control by oxidation and reduction.
D000150:Acinetobacter / Q000201:enzymology*; D008058:Dihydrolipoamide Dehydrogenase / Q000037:antagonists & inhibitors / Q000145:classification / Q000302:isolation & purification; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D014755:Viologens / Q000378:metabolism
D014755:Viologens; D009243:NAD; D009247:NADH, NADPH Oxidoreductases; D008058:Dihydrolipoamide Dehydrogenase