ISSN:
1399-3054
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
During oxidation of indole-3-acetic acid catalyzed by horseradish peroxidase, indole-3-aldehyde and 3-hydroxymethayloxindole cease to be produced a few minutes after initiation of the reaction even though IAA is still being consumed. At the same time an increased accumulation of indole-3-methanol is observed and the ratio of oxygen to indole-3-acetic acid consumed becomes less than unity. Indole-3-niethanol can be a substrate for horseradish peroxidase provided that H2O2 is present. In this reaction, indole-3-aldehyde but not 3-hydroxymethyloxindole is formed. H2O2 is not merely an activating agent for the enzyme but also a true oxidant because it is consumed stoichiometrically (1 mol of H2O2 per mol of indole-3-methanol) and the reaction is independent of the presence of oxygen. Indole-3-methanol is proposed as an intermediate in the process of oxidation of indole-3-acetic acid into indole-3-al-denyde, the second step of which requires peroxide as an oxidant.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1399-3054.1983.tb00732.x
