The oxidation of indoe-3-acetic acid by anionic tomato peroxidase was found to be neglUige unless reaction mixtures were supplemented with H202. The addition of H202 to reaction mixtures initiated a period of rapid indole-3-acetic acid oxidation and 02 uptake; this phase ended and 02 uptake fell to a low level when the H202 was exhausted. The stoichiometry of the reaction, which is highly dependent on enzyme concentration and pH, suggests that H202 initiates a sequence of reactions in which indole-3-acetic acid is oxidized.Many plant peroxidases catalyze the oxidation of IAA by molecular 02 in the presence of a phenol and manganous ion (2,6,10,14,16
MATERIALS AND METHODSEnzyme Source and Estimation. Tomato anionic peroxidase was extracted from tomato (Lycopersicon esculentum var. tropic) pericarp tissue and purified to about 85% homogeneity as previously described (11). Enzyme concentrations were estimated from the 403 nm A of solutions, using a millimolar extinction coefficient of 107 for the enzyme (11). A spectra from 400 nm to 600 nm wavelength were run on a Perkin-Elmer 124 spectrophotometer and associated chart recorder and used to determine if the enzyme was present as ferric enzyme, ferrous enzyme, compound I, compound II, or compound III (11