ABSTRACT
The relation between microenvironment and the tertiary structure of cytochrome P-450 LM2 has been investigated. No complete relaxation to the most active state of the native enzyme took place in the case of membrane-incorporated hemoprotein with three or four intramolecular cross-links. The spatial organization of the enzyme was predicted to determine the cross-link location on the hemoprotein surface and membrane-incorporated parts of the polypeptide chain. It was concluded on the basis of the predicted structure that hemoprotein has an amphipathic structure and, thus, the greater part of molecule is exposed to the water phase. Not more than one NH2-terminal alpha helix is able to incorporate into the membrane. The location of this region is believed to control the formation of the catalytically-active-conformational state of cytochrome P-450 LM2.
