Free radical formation in the oxidation of malondialdehyde and acetylacetone by peroxidase enzymes.
Malondialdehyde, a product of lipid peroxidation, and acetylacetone undergo one-electron oxidation by peroxidase enzymes to form free radical metabolites, which were detected with ESR using the spin-trapping technique. The structures of the radical adducts were assigned using isotope substitution. With both malondialdehyde and acetylacetone and the enzymes myeloperoxidase and chloroperoxidase, carbon-centered radicals were detected. With horseradish peroxidase, a carbon-centered radical was initially trapped and then disappeared with the concomitant appearance of an iminoxyl radical.
Mottley
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Laboratory of Molecular Biophysics, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.
Robinson
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Mason
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D002711:Chloride Peroxidase / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008315:Malondialdehyde / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010422:Pentanones / Q000378:metabolism*; D009195:Peroxidase / Q000378:metabolism*
D005609:Free Radicals; D010422:Pentanones; C008790:acetylacetone; D008315:Malondialdehyde; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase; D009195:Peroxidase