[Comparative study of NADP-reductase properties in two species of purple bacteria].
Unlike Rhodospirillum rubrum, the highly purified preparations of NADP-reductase Thiocapsa roseopersicina are capable of reduction of cytochrome c though they do not catalyse diaphorase reaction in the presence of methyl viologen or benzyl viologen and NADH. T. roseopersicina reductase has more high temperature optimum (50-65 degrees) and more high thermal stability (65 degrees) and it is capable to catalyse diaphorase and menadione-reductase reactions under more high pH values (11.0-12.0) than NADP-reductase of R. rubrum. NADP-reductase of T. roseopersicina is more stable under storing than the enzyme from R. rubrum: the semi-inactivation period of the enzyme when storing in Ar or the air is about 10 and 4 days, respectively, and it takes about three days for R. rubrum.
D001128:Argon; D003579:Cytochrome Reductases / Q000378:metabolism*; D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism; D004355:Drug Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D011808:Quinone Reductases / Q000378:metabolism; D012245:Rhodospirillales / Q000201:enzymology*; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D013045:Species Specificity; D014755:Viologens / Q000494:pharmacology
D014755:Viologens; D001128:Argon; D003579:Cytochrome Reductases; D009251:NADPH-Ferrihemoprotein Reductase; D011808:Quinone Reductases; D008058:Dihydrolipoamide Dehydrogenase
Sravnenie svoĭst' NADP-reduktazy u dvukh vidow purpurnykh bakteriĭ.