[Purification and properties of NADP-reductase of phototropic bacteria Thiocapsa roseopersicina].
The method of purification up to homogenous states and properties of NADP-reductase of purple bacteria Thiocapsa roseopersicina, strain BBS, are described. The molecular weight of NADP-reductase is about 47 000; it is flavoprotein consisting of two subunits. Atebrim and chloromercury bensoate inhibit the activity of NADP-reductase (34% and 33--60%, respectively). The enzyme is specific to NADPH; it catalyzes menadion-reductase reaction, diaphorase reaction of benzyl viologen reduction, oxidation of reduced benzyl viologen in the presence of NADP, reduction of ferredoxin and cytochrome c in the presence of NADPH, but it is not capable to catalyze transhydrogenase reaction.
D002841:Chromatiaceae / Q000201:enzymology*; D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism; D005420:Flavoproteins / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D009249:NADP / Q000494:pharmacology; D011808:Quinone Reductases / Q000378:metabolism; D013329:Structure-Activity Relationship
D005420:Flavoproteins; D046911:Macromolecular Substances; D009249:NADP; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases; D008058:Dihydrolipoamide Dehydrogenase
Ochistka i svoĭstva NADP-reduktazy iz fototrofnoĭ bakterii Thiocapsa roseoppersicina.