The comparative study of peroxidase activity and substrate binding properties of cytochrome P450 2B4 incorporated into phospholipid vesicles with the use of two different methods.
The comparative study of peroxidase activities and substrate binding properties of cytochrome p450 2B4 in reconstituted vesicles prepared with the use of two different techniques, and microsomal cytochrome P450 was carried out. The data obtained show that the two types of cytochrome P450 2B4-containing proteoliposomes do not differ substantially from each other with respect to H2O2- or cumene hydroperoxide-dependent substrate hydroxylation activities as well as substrate binding properties of hemoprotein reconstituted. However, some parameters measured with proteoliposomal cytochrome P450 are markedly different from those measured with microsomal hemoprotein, suggesting the existence of conformational differences between the molecules of these two cytochromes or the differences in the depth of their immersion into lipid bilayer.
Apletalina
E V
EV
Institute of Biomedical Chemistry, Russia Academy of Medical Sciences, Moscow, Russia.
Yakousheva
E A
EA
Uvarov VYu
Popenko
V I
VI
Archakov
A I
AI
D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D003956:Dialysis; D006861:Hydrogen Peroxide / Q000378:metabolism; D006900:Hydroxylation; D007700:Kinetics; D008081:Liposomes; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology; D011817:Rabbits; D013250:Steroid Hydroxylases / Q000378:metabolism*; D013379:Substrate Specificity
D008081:Liposomes; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide; D013250:Steroid Hydroxylases; D001189:Aryl Hydrocarbon Hydroxylases; C019781:benzphetamine N-demethylase; C050356:steroid 15-alpha-hydroxylase; D010089:Oxidoreductases, N-Demethylating; D010634:Phenobarbital