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Indole‐3‐methanol as an intermediate in the oxidation of indole‐3‐acetic acid by peroxidase
Author(s) -
Sabater Francisco,
Acosta Manuel,
SánchezBravo José,
Cuello Juan,
Rio José A.
Publication year - 1983
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1983.tb00732.x
Subject(s) - indole test , horseradish peroxidase , indole 3 acetic acid , methanol , chemistry , substrate (aquarium) , acetic acid , peroxidase , aldehyde , medicinal chemistry , organic chemistry , catalysis , enzyme , biochemistry , biology , ecology , auxin , gene
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 H 2 O 2 is present. In this reaction, indole‐3‐aldehyde but not 3‐hydroxymethyloxindole is formed. H 2 O 2 is not merely an activating agent for the enzyme but also a true oxidant because it is consumed stoichiometrically (1 mol of H 2 O 2 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.