On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction.
LD Gorsky, DR Koop, MJ Coon - Journal of Biological Chemistry, 1984 - ASBMB
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 …
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 …