Abstract The aromatic ring of dihydroxyphenylpropanoids was found to be cleaved by two types of highly characterized crystalline oxygenases derived from bacteria. Oxidation of caffeic acid, chlorogenic acid, dihydroxyphenylalanine, and dihydroxyphenylethylamine by the intradiol and extradiol-cleaving enzymes, protocatechuate 3,4-dioxygenase and metapyrocatechase, respectively, permits description of rates and characteristics of the cleavage reactions and spectral properties of the products. The described reactions and oxidation products are pertinent to the study of plant aromatic metabolism and the degradation of plant constituents by soil bacteria.
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