Thyroid peroxidase selects the mechanism of either 1- or 2-electron oxidation of phenols, depending on their substituents.
Unlike lactoperoxidase and horseradish peroxidase, thyroid peroxidase catalyzed the oxidation of hydroquinone mostly by way of 2-electron transfer. This conclusion could be derived from three independent experiments: ESR measurements of p-benzosemiquinone, trapping the unpaired electron by cytochrome c, and spectrophotometric analysis of catalytic intermediates of the enzymes. The 1-electron flux for hydroquinone oxidation was found to be 15-19% in the reaction of thyroid peroxidase, while it was nearly 100% in the reactions of lactoperoxidase and horseradish peroxidase. From the spectrophotometric analysis of the catalytic intermediates of enzyme, it was suggested that the mechanism of oxidation catalyzed by thyroid peroxidase changes from a 2-electron to a 1-electron type as the substituents at 2- and 6-positions of phenol become bulky or heavy. On the other hand, the mechanism was invariably a 1-electron type when the oxidation of phenols was catalyzed by lactoperoxidase or horseradish peroxidase. These three peroxidases all catalyzed 1-electron oxidation of ascorbate.
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D006873:Hydroquinones; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000494:pharmacology*; D010636:Phenols; D013329:Structure-Activity Relationship; D013552:Swine; D013961:Thyroid Gland / Q000201:enzymology*
D006873:Hydroquinones; D010636:Phenols; D010544:Peroxidases; C031927:hydroquinone