[Reconstitution of the monooxygenase system in a solution and in an immobilized phospholipid layer].
To clarify the molecular organization of NADH- and NADPH-dependent microsomal redox systems their isolated purified carriers were incorporated into immobilized azolectin layer with a higher viscosity than that of the liposomes. It was shown that the NADH-cytochrome c reductase activity characterizing the NADH-cytochrome b5 reductase and cytochrome b5 interaction sharply decreased in the immobilized system as compared to that in solution. However, the activity of hydroxylase reactions catalyzed by immobilized NADPH-cytochrome P-450 reductase and cytochrome P-450 was the same as in solution. This, the reconstitution in the immobilized phospholipid layer allowed to characterize NADH-cytochrome b5 reductase as a system operating on occasional collisions of its components. On the contrary, the diffusion of the NADPH-dependent redox chain carriers was not the rate-limiting step of the reaction.
D000818:Animals; D003579:Cytochrome Reductases / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism*; D008560:Membrane Fluidity; D008862:Microsomes, Liver / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D011817:Rabbits; D012996:Solutions; D014783:Viscosity
D008051:Lipid Bilayers; D010743:Phospholipids; D012996:Solutions; D003579:Cytochrome Reductases; D009251:NADPH-Ferrihemoprotein Reductase; D009245:NADH Dehydrogenase
Rekonstruktsiia monooksigenaznoĭ sistemy v rastvore i v immobilizovannom sloe fosfolipida.