Oxidation of p-aminophenol catalyzed by horseradish peroxidase and prostaglandin synthase.
p-Aminophenol oxidation is catalyzed by horseradish peroxidase. ESR spectroscopy demonstrates the formation of the p-aminophenoxy free radical, the one-electron oxidation product of p-aminophenol. The same radical is formed by alkaline autoxidation of this compound. The ultimate products of p-aminophenol oxidation are mainly polymeric; however, indophenol was isolated in low yield. Oxidation of p-aminophenol is also catalyzed by the hydroperoxidase activity of prostaglandin synthase, using ram seminal microsomal preparations as the enzyme source.
D000627:Aminophenols / Q000378:metabolism*; D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D006735:Horseradish Peroxidase / Q000378:metabolism*; D008297:Male; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism*; D012756:Sheep
D000627:Aminophenols; D006735:Horseradish Peroxidase; D010544:Peroxidases; D011451:Prostaglandin-Endoperoxide Synthases; C026729:4-aminophenol