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JBC, Vol. 251, Issue 10, 3045-3051, May, 1976
B. Goldberg, A. Stern and J. Peisach
The mechanism by which superoxide anion is generated by the interaction of
phenylhydrazine with either oxy- or methemoglobin was investigated. Rather
than superoxide anion generation resulting from an accelerated
autooxidation of oxyhemoglobin, it was found that both oxy- and
methemoglobin function as peroxidases toward phenylhydrazine with the
resultant oxidation of this compound to phenyldiazine. Generation of
phenyldiazine from the oxidation of phenylhydrazine by hemoglobin or by the
hydrolysis and subsequent decarboxylation of methyl phenylazoformate
(C6H5N=NCOOCH3) resulted in the production of superoxide anion. It is
suggested that under certain conditions hemoglobin may function as a
drug-metabolizing peroxidase.
The mechanism of superoxide anion generation by the interaction of phenylhydrazine with hemoglobin
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