The involvement of superoxide anions in the autoxidation of various cofactors of cysteamine-oxygenase.
The reduction of tetranitroblue tetrazolium with cysteamine, mediated by a number of dyes, elemental sulphur, elemental selenium and selenide, under aerobic conditions, was inhibited to various extent upon addition of superoxide dismutase. A strict parallelism between the ability to produce O2- ions and the property of those compounds to act as cofactors for cysteamine-oxygenase, to yield hypotaurine, has been observed. Based on the fact that the autoxidation of cysteamine also gives rise to O2- formation, though to a minor extent, we propose a mechanism for cysteamine-oxygenase action. This mechanism was derived from the data obtained in the model system studied.
D000818:Animals; D002417:Cattle; D003543:Cysteamine; D004579:Electron Transport; D004912:Erythrocytes / Q000201:enzymology; D007700:Kinetics; D009580:Nitroblue Tetrazolium; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000097:blood; D013481:Superoxides
D013481:Superoxides; D009580:Nitroblue Tetrazolium; D003543:Cysteamine; D010105:Oxygenases; D013482:Superoxide Dismutase