Covalent binding to apoprotein is a major fate of heme in a variety of reactions in which cytochrome P-450 is destroyed.

F P Guengerich

Index: Biochem. Biophys. Res. Commun. 138(1) , 193-8, (1986)

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Abstract

The heme in rat liver microsomal cytochrome P-450 was labeled with 14C or 3H and the microsomes were fractionated after in vitro incubations with a variety of agents known to destroy cytochrome P-450 heme. A major fraction of the heme label was irreversibly bound to apoprotein in all cases, including incubations with fluroxene, 1-octene, vinyl bromide, trichloroethylene, vinyl chloride, parathion, cumene hydroperoxide, NaN3, or iron-ADP complex. Label was also extensively bound to apoprotein when purified and reconstituted cytochrome P-450 was incubated with NADPH and vinyl chloride. This process appears to be widespread and involved to a significant extent in the cytochrome P-450 heme destruction observed with many compounds.