Autoinactivation of xanthine oxidase: the role of superoxide radical and hydrogen peroxide.
Xanthine oxidase suffers autoinactivation in the course of catalyzing the oxidation of acetaldehyde. When no special efforts were made to maintain a high pO2 in these reaction mixtures catalase protected the xanthine oxidase, but superoxide dismutase did not. However, when oxygen depletion was slowed or prevented by working at lower concentrations of xanthine oxidase, at lower temperatures or by vigorous agitation under an atmosphere of 100% oxygen, superoxide dismutase or catalase protected markedly when added separately and protected almost completely when added together. This result correlates with the greater production of O2-, relative to H2O2, by xanthine oxidase, at elevated pO2. Since histidine also provided some protection and the high levels of acetaldehyde used would have precluded any significant effect of OH., we conclude that singlet oxygen, or something with similar reactivity, was generated from O2- plus H2O2 and contributed significantly to the observed autoinactivation.
D006639:Histidine / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D008353:Mannitol / Q000494:pharmacology; D010100:Oxygen / Q000494:pharmacology*; D013481:Superoxides / Q000494:pharmacology*; D014969:Xanthine Oxidase / Q000037:antagonists & inhibitors*
D013481:Superoxides; D008353:Mannitol; D006639:Histidine; D006861:Hydrogen Peroxide; D014969:Xanthine Oxidase; D010100:Oxygen