Add time:07/28/2019         Source:sciencedirect.com

Horse-radish peroxidase catalyzes the oxidation of homogentisic acid in the presence of sulfhydryl compounds to form products similar to those obtained by the spontaneous reaction of benzoquinoneacetic acid with sulfhydryl agents. Other heme proteins, such as catalase, cytochrome c, hemoglobin and methemoglobin, do not catalyze this oxidation. Studies on substrate specificity have indicated that a number of aromatic compounds containing disubstituted hydroxy or amino groups in the para position are oxidized in this system. A scheme is presented illustrating a mechanism to explain the formation of thioether derivatives of homogentisic acid and sulfhydryl agents in the presence of horse-radish peroxidase. Similar reactions may be involved in the formation of ochronotic pigment in the connective tissues of alcaptonuric subjects or after topical application of phenol or resorcinol.

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