Abstract
The monooxygenase system of the endoplasmic reticulum of liver cells is of great importance to the production of reactive metabolites from xenobiotics, and in recent years there has been a good deal of interest in attempting to discover the molecular organization of this enzyme system in the membrane (Peterson et al., 1976, 1978; Yang, 1975, 1977). The system comprises two protein components: (i) cytochrome P-450 reductase and (ii) cytochrome P-450. The function of cytochrome P-450 reductase is to bring about the transfer of electrons from NADPH to the terminal oxidase of the system, cytochrome P-450, which binds both the xenobiotic substrate and molecular oxygen. Unlike the reductase, cytochrome P-450 exists in a number of distinct forms, each of which demonstrates different characteristics with respect to substrate preference and catalytic parameters.
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