| Abstract: | 1-Naphthol was metabolised by horseradish peroxidase (HRP) in a H2O2-dependent reaction to methanol-soluble and covalently bound products. Spectrophotometric and electron spin resonance (ESR) studies established that HRP catalysed the one electron oxidation of 1-naphthol to naphthoxy or a naphthoxy-derived radical. Inclusion of glutathione (GSH) in the reaction caused a dose-dependent inhibition of covalent binding and an increase in the amount of unmetabolised 1-naphthol present at the end of the incubation. gamma-Radiolysis studies suggest that this is due to the reduction of naphthoxy radicals by GSH yielding 1-naphthol and GS.. In agreement with this, HRP-catalysed-oxidation of 1-naphthol in the presence of GSH, was found to stimulate oxidised glutathione (GSSG) formation. |
