Peroxidase activation of 1-naphthol to naphthoxy or naphthoxy-derived radicals and their reaction with glutathione.
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.
D004305:Dose-Response Relationship, Drug; D004578:Electron Spin Resonance Spectroscopy; D005720:Gamma Rays; D005978:Glutathione / Q000494:pharmacology; D006735:Horseradish Peroxidase / Q000378:metabolism*; D009284:Naphthols / Q000378:metabolism* / Q000528:radiation effects; D010544:Peroxidases / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
D009284:Naphthols; C029350:1-naphthol; D006735:Horseradish Peroxidase; D010544:Peroxidases; D005978:Glutathione