Circular dichroism of partially purified cytochrome P-450 from rabbit liver microsomes.
The heme related circular dichroic bands of solubilized cytochrome P-450 from rabbit liver and some of its complexes with type I- and type II-substrayes and heme iron ligands were measured in the Soret region. All P-450 dersorption. The positions of the dichroic bands together with their ellipticities vary with ligand substitution and the oxidative state of the iron. The results are compared with CD-date of other hemoproteins and discussed with respect to stereochemical properties of the heme pocket.
D000818:Animals; D002942:Circular Dichroism; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D006418:Heme / Q000032:analysis; D008099:Liver / Q000032:analysis*; D008862:Microsomes, Liver / Q000032:analysis*; D011817:Rabbits
D006418:Heme; D003577:Cytochrome P-450 Enzyme System