Abstract
The mechanism of liver microsomal aromatic hydroxylation has been investigated by using cumene hydroperoxide as the hydroxylating agent and comparing this reaction with the NADPH-dependent reaction. The conversion of [4-(3)H]acetanilide to 4-hydroxyacetanilide by rat liver microsomes (or purified cytochrome P-450) in the presence of either cumene hydroperoxide or NADPH is attended by comparable 'NIH shifts'. This indicates that hydroxylation in the two systems proceeds via a common intermediate, presumably an arene oxide. The intermediacy of an arene oxide, phenanthrene-9,10-oxide, is established by incubating [3-(3)H]-phenanthrene with rat-liver microsomes and cumene hydroperoxide in the presence of either non-radioactive phenanthrene-9,10-oxide as a 'trap' or in the presence of cyclohexene oxide, an inhibitor of the enzyme epoxide hydrase. Incubation of phenanthrene with cumene hydroperoxide in an 18O-enriched medium has confirmed that the oxygen atom in phenanthrene-9,10-oxide is derived from the hydroperoxide and not from the medium.
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