[Purification and properties of NADP-reductase of phototropic bacteria Thiocapsa roseopersicina]

Autor: I N, Gogotov, T V, Laurinavichene
Rok vydání: 1977
Předmět:
Zdroj: Biokhimiia (Moscow, Russia). 42(7)
ISSN: 0320-9725
Popis: 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.
Databáze: OpenAIRE