Mechanism for the generation of superoxide anion and singlet oxygen during heme compound-catalyzed linoleic acid hydroperoxide decomposition

Arch Biochem Biophys. 1991 Sep;289(2):223-9. doi: 10.1016/0003-9861(91)90465-u.

Abstract

Heme compound, hematin or cytochrome c, catalyzes the decomposition of 13-hydroperoxy linoleic acid yielding both O2- and 1O2 under aerobic conditions. No 1O2 is produced when hydrogen peroxide and cumene hydroperoxide are used as substrates. In these experiments, both O2- and 1O2 could be precisely detected by a chemiluminescence method using a cypridina luciferin analog, 2-methyl-6-(p-methoxyphenyl)-3,7-dihydroimidazo[1,2-a]pyrazin++ +-3-one, as a chemiluminescence probe, in the absence and presence of Cu-Zn superoxide dismutase in catalytic amounts. The reduction and oxidation cycle of ferric heme compound and the bimolecular reaction of peroxyl radicals are plausible reaction mechanisms for O2- and 1O2 production, respectively, in the systems studied.

MeSH terms

  • Catalysis
  • Heme / metabolism*
  • Imidazoles
  • In Vitro Techniques
  • Linoleic Acids / metabolism
  • Lipid Peroxides / metabolism
  • Luminescent Measurements
  • Oxidation-Reduction
  • Oxygen / metabolism*
  • Pyrazines
  • Singlet Oxygen
  • Superoxides / metabolism*

Substances

  • Imidazoles
  • Linoleic Acids
  • Lipid Peroxides
  • Pyrazines
  • Superoxides
  • 2-methyl-6-(4-methoxyphenyl)-3,7-dihydroimidazo(1,2-alpha)pyrazin-3-one
  • Singlet Oxygen
  • linoleic acid hydroperoxide
  • Heme
  • Oxygen