Nitroxide-stimulated H2O2 decomposition by peroxidases and pseudoperoxidases

• Published in: Free radical research communications Vol. 17; no. 3; p. 157
• Main Authors: Mehlhorn, R J, Swanson, C E
• Format: Journal Article
• Language: English
• Published: Switzerland 1992
• Subjects: Ascorbic Acid - pharmacology; Catalysis; Electron Spin Resonance Spectroscopy; Free Radical Scavengers; Free Radicals; Glutathione - pharmacology; Hemoglobins - drug effects; Hemoglobins - metabolism; Hydrogen Peroxide - metabolism; Myoglobin - drug effects; Myoglobin - metabolism; Nitrogen Oxides; Oxidation-Reduction; Oxygen - metabolism; Peroxidases - antagonists & inhibitors; Peroxidases - metabolism; Structure-Activity Relationship
• ISSN: 8755-0199
• DOI: 10.3109/10715769209068163

Nitroxide free radicals interact with Hb/metHb, Mb/metMb and with peroxidases/phenols to induce a catalase-like conversion of H2O2 to O2 (catalatic activity), without being substantially consumed in the process. The mechanism of this reaction is postulated to involve a one-electron oxidation of the nitroxide to the immonium oxene, which then reacts further to release oxygen and the nitroxide. An involvement of the immonium oxene in the reaction mechanism is consistent with ferryl heme reduction by nitroxides and a detection of the reduced nitroxide when the reaction mixture is supplemented with the two-electron reductant sodium borohydride. The nitroxide-induced catalatic activity is completely inhibited when the reaction mixture is supplemented with glutathione. Nitroxides suppress free radical formation by hydroperoxide-activated heme proteins, as inferred from their inhibition of the spin-trapping of glutathionyl radicals. H2O2 decomposition and a suppression of reactive free radical formation by heme proteins appears to be an antioxidant activity of nitroxides, which is distinct from their previously reported superoxide dismutating activity and which may be a factor in their protective action in models of cardiac reperfusion injury.