An electron spin resonance study of the activation of benzidine by peroxidases.
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 electron spin resonance 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.
D001560:Benzidines / Q000378:metabolism*; D001711:Biotransformation; D004578:Electron Spin Resonance Spectroscopy; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D013053:Spectrophotometry
D001560:Benzidines; C029876:benzidine; D006735:Horseradish Peroxidase; D010544:Peroxidases