THE ENZYMICALLY CATALYZED OXIDATION OF INDOLEACETIC ACID

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Abstract
Dialyzed wheat leaf extracts, catalase, and horse-radish peroxidase catalyze the decarboxylation and oxidation of indoleacetic acid at pH 5.0–6.0 in the presence of critical concentrations of manganese and monohydric phenols or resorcinol. The equivalent of 1 mole of carbon dioxide is liberated and 1 mole of oxygen consumed per mole of substrate. Manganic ions formed by a phenol–peroxidase–peroxide system initiate the decarboxylation and oxidation. A naturally occurring ether soluble factor from wheat leaves, and maleic hydrazide, can substitute for the active phenols. Catechol, hydroquinone, pyrogallol, seopoletin, and riboflavin, etc. competitively inhibit the oxidation. The nature of the active peroxide is discussed and a reaction sequence involving an organic peroxide or radical rather than hydrogen peroxide is submitted as being a possibility.