[Conformational state and functional activity of NADPH-dependent cytochrome P-450 reductase isolated and incorporated into phospholipid bilayers].
It was shown that the alpha-helix content in both isolated and incorporated into phospholipid bilayer NADPH-dependent cytochrome P-450 reductase is 20%. NADPH or dithionite reduction of the flavoprotein is not followed by conformational changes. The incorporation of the NADPH-dependent cytochrome P-450 reductase molecule into the phospholipid bilayer does not affect its catalytic properties. It was found that the protein does not interact with the phospholipid bilayer of phosphatidyl choline liposomes but incorporates readily into the liposomal membrane from a microsomal phospholipid mixture with a binding constant of 17.4 microM.
D000818:Animals; D004227:Dithionite / Q000494:pharmacology; D007425:Intracellular Membranes / Q000502:physiology; D007700:Kinetics; D008051:Lipid Bilayers; D008563:Membrane Lipids / Q000502:physiology; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010713:Phosphatidylcholines / Q000494:pharmacology; D011487:Protein Conformation; D011817:Rabbits
D008051:Lipid Bilayers; D008563:Membrane Lipids; D010713:Phosphatidylcholines; D004227:Dithionite; D009251:NADPH-Ferrihemoprotein Reductase
Konformatsionnoe sostoianie i funktsional'naia aktivnost' izolirovannoĭ i vstroennoĭ v fosfolipidnyĭ bisloĭ NADPH-zavisimoĭ tsitokhrom P-450 reduktazy.