AN ELECTRON-SPIN RESONANCE STUDY OF THE ACTIVATION OF BENZIDINE BY PEROXIDASES
- 1 January 1983
- journal article
- research article
- Vol. 23 (3) , 766-770
Abstract
The oxidation of benzidine, a carcinogenic aromatic amine, by H2O2 is catalyzed by horseradish peroxidase or lactoperoxidase. The resulting cation free radical is moderately stable at pH 5.0, and was identified by ESR spectroscopy. Two-electron oxidation yields the benzidine di-imine. This species reacts with phenol or catechol derivatives to give colored adducts. Monoacetylbenzidine is a relatively poor peroxidase substrate, and the biological implications of this difference are discussed.This publication has 10 references indexed in Scilit:
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