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  • Title: [Purification and properties of NADP-reductase of phototropic bacteria Thiocapsa roseopersicina].
    Author: Gogotov IN, Laurinavichene TV.
    Journal: Biokhimiia; 1977 Jul; 42(7):1285-91. PubMed ID: 20166.
    Abstract:
    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.
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