[Regulation mechanisms of the endoplasmic cytochrome P-450 systems of the liver].

Regulation mechanisms of the cytochrome P-450 dependent monooxygenase from the hepatic endoplasmic reticulum at 3 different integrational levels are discussed. At the molecular level the activity of the system is regulated by a substrate dependent shift of an equilibrium of cytochrome P-450 spin conformers in favour of the high spin component. A correlation between the extent of the spin shift, the reduction rate and the substrate turnover has been evidenced. The regulation at the membrane level is based on interactions between the 3 essential components of the system: cytochrome P-450, reductase and lipid. The formation of the cytochrome P-450-reductase-complex necessary for oxygen activation by transfer of electrons is dependent on the charge of the phospholipids. The binding constant of the donor-acceptor complex increases with the acidity of the phospholipid head group, thus enhancing the velocity of the electron transfer.