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.