Dichlorobenzidine-DNA binding catalyzed by peroxidative activation in Salmonella typhimurium.

Peroxidative oxidation of dichlorobenzidine in vitro results in covalent binding to exogenous DNA. In a modified Ames assay, mutagenicity is observed in S. typhimurium strain TA98 following the incubation of dichlorobenzidine, bacteria, and hydrogen peroxide. In this paper, we demonstrate that [14C]dichlorobenzidine becomes covalently bound to S. typhimurium macromolecules, including DNA, when exogenous hydrogen peroxide is supplied. We compared the levels of binding in a pair of otherwise isogenic strains with wild-type (oxyR+) versus constitutive (oxyR1) expression of the hydrogen peroxide stress-induced regulon. Binding was approximately twofold higher in TA4124 (oxyR1) than in TA4123 (oxyR+). Bacterial hydroperoxidases may catalyze the activation of dichlorobenzidine to mutagenic and DNA binding species in this system.