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J. Biol. Chem., Vol. 259, Issue 11, 6812-6817, Jun, 1984
LD Gorsky, DR Koop and MJ Coon
This laboratory has recently reported that, in a reconstituted enzyme
system containing alcohol-induced isozyme 3a of liver microsomal cytochrome
P-450, the sum of acetaldehyde generated by the monooxygenation of ethanol
and of hydrogen peroxide produced by the NADPH oxidase activity is
inadequate to account for the O2 and NADPH consumed. Studies on the
stoichiometry have revealed the occurrence of an additional reaction
involving an overall 4-electron transfer to molecular oxygen which is
presumed to yield water: O2 + 2 NADPH + 2H+--- -2 H2O + 2 NADP+. The
occurrence of a peroxidase reaction in which free H2O2 is reduced to water
by NADPH was ruled out. When the 4-electron oxidase activity is taken into
account, measurements of NADPH oxidation and O2 consumption are in accord
with the amounts of products formed in the presence of various P-450
isozymes, either in the absence or presence of typical substrates,
including those which undergo hydroxylation, N- or O-demethylation, or
oxidation of hydroxymethyl to aldehyde groups. Of the substrates examined,
some had no effect on the oxidase reaction yielding hydrogen peroxide or
the 4-electron oxidase reaction, some were inhibitory, and some were
stimulatory, but the same substrate did not necessarily have the same
effect on the two reactions.
On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction
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