Oxidation of uroporphyrinogens by hydroxyl radicals. Evidence for nonporphyrin products as potential inhibitors of uroporphyrinogen decarboxylase.
A hydroxyl radical-generating system, hypoxanthine/xanthine oxidase/Fe-EDTA, oxidises uroporphyrinogens to uroporphyrins and to more polar nonporphyrin products. The evidence suggests that the nonporphyrin products have inhibitory activity towards mouse liver uroporphyrinogen decarboxylase which could explain some forms of human and experimental porphyrias.
Francis
J E
JE
MRC Toxicology Unit, Medical Research Council Laboratories, Carshalton, England.
Smith
A G
AG
D000818:Animals; D002250:Carbon Radioisotopes; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors*; D005609:Free Radicals; D006801:Humans; D006878:Hydroxides; D017665:Hydroxyl Radical; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D051379:Mice; D010084:Oxidation-Reduction; D011164:Porphyrias / Q000201:enzymology; D011165:Porphyrinogens; D014575:Uroporphyrinogen Decarboxylase / Q000037:antagonists & inhibitors*; D014577:Uroporphyrinogens
D002250:Carbon Radioisotopes; D005609:Free Radicals; D006878:Hydroxides; D011165:Porphyrinogens; D014577:Uroporphyrinogens; D017665:Hydroxyl Radical; D002262:Carboxy-Lyases; D014575:Uroporphyrinogen Decarboxylase