Faculty Publications

Inhibition of veratryl alcohol oxidase activity of lignin peroxidase H2 by 3-amino-1,2,4-triazole

Document Type

Article

Journal/Book/Conference Title

Archives of Biochemistry and Biophysics

Volume

293

Issue

2

First Page

287

Last Page

291

Abstract

The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was inhibited by 3-amino-1,2,4-triazole (AT). Inhibition was found to be competitive with respect to veratryl alcohol (KI = 18 μM) and noncompetitive with respect to H2O2. Unlike bovine lactoperoxidase, catalase, and thyroid peroxidase, AT was not a suicide (mechanism based) inhibitor for lignin peroxidase H2. Binding studies revealed that lignin peroxidase H2 catalyzed insignificant binding of [14C]AT to the enzyme. Apparently AT is a poor substrate for lignin peroxidase H2 and is only slowly oxidized to form a yellow product in the presence of H2O2. The formation of the yellow product was shown to increase with increasing concentrations of veratryl alcohol, suggesting that an intermediate in the oxidation of veratryl alcohol is able to mediate the oxidation of AT. Extensive metabolism of AT to CO2 by the white rot fungus Phanerochaete chrysosporium (∼60% in 30 days) was also demonstrated. © 1992.

Original Publication Date

1-1-1992

DOI of published version

10.1016/0003-9861(92)90397-F

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