Cysteamine oxygenase: possible involvement of superoxide ion in the catalytic mechanism

Free Radic Res Commun. 1987;3(6):365-71. doi: 10.3109/10715768709088077.

Abstract

The reaction catalyzed by cysteamine oxygenase on cysteamine in the presence of phenazine methosulphate as cofactor like compound is inhibited by nitroblue tetrazolium, a scavenger of superoxide ions. The reaction is not inhibited by superoxide dismutase and allyl alcohol and it is not activated by superoxide ions produced in solution. Nitroblue tetrazolium is reduced by cysteamine or mercaptoethanol and phenazine methosulphate. This reaction is completely inhibited by superoxide dismutase. In the presence of cysteamine oxygenase the reduction with mercaptoethanol is greatly enhanced and it is only partially inhibited by superoxide dismutase. According to these data a reaction mechanism is proposed in which superoxide ions and thiyl radicals are produced at the active site during catalysis.

MeSH terms

  • 1-Propanol / pharmacology
  • Catalysis
  • Cysteamine / pharmacology
  • Dioxygenases*
  • Free Radicals
  • Mercaptoethanol / pharmacology
  • Methylphenazonium Methosulfate / pharmacology
  • Nitroblue Tetrazolium / metabolism
  • Oxidation-Reduction
  • Oxygenases / metabolism*
  • Propanols
  • Superoxide Dismutase / pharmacology
  • Superoxides / metabolism*

Substances

  • Free Radicals
  • Propanols
  • Superoxides
  • Nitroblue Tetrazolium
  • Methylphenazonium Methosulfate
  • allyl alcohol
  • Cysteamine
  • Mercaptoethanol
  • 1-Propanol
  • Oxygenases
  • Dioxygenases
  • cysteamine dioxygenase
  • Superoxide Dismutase