[The role of heme in formation of the native structure of cytochrome P-450 LM2].
The role of heme in the formation of cytochrome P-450 native structure was investigated. It was shown that treatment of purified and membrane-bound hemoproteins with H2O2 results in the total destruction of heme. After incubation with hemine the apoprotein thus obtained forms a catalytically active cytochrome P-450. The efficiency of this process depends on the enzyme microenvironment. The membrane-bound apoprotein may be reconstituted by 70-80%, whereas the soluble one--by 50%. It is concluded that the observed differences may be accounted for by a greater stability of the membrane-bound protein structure.
Uvarov
V Iu
VIu
Tret'iakov
V E
VE
Kuznetsova
G P
GP
Archakov
A I
AI
D000818:Animals; D001051:Apoenzymes / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology; D011487:Protein Conformation; D011817:Rabbits
D001051:Apoenzymes; D007527:Isoenzymes; D008565:Membrane Proteins; D006418:Heme; D003577:Cytochrome P-450 Enzyme System
Rol' gema v formirovanii nativnoĭ struktury tsitokhroma P-450 LM2.