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.