@article{ref1,
title="Inhibition of veratryl alcohol oxidase activity of lignin peroxidase H2 by 3-amino-1,2,4-triazole",
journal="Archives of biochemistry and biophysics",
year="1992",
author="Tuisel, H. and Grover, T. A. and Bumpus, J. A. and Aust, S. D.",
volume="293",
number="2",
pages="287-291",
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 (K1 = 18 microM) 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 (approximately 60% in 30 days) was also demonstrated.<p /><p>Language: en</p>",
language="en",
issn="0003-9861",
doi="10.1016/0003-9861(92)90397-f",
url="http://dx.doi.org/10.1016/0003-9861(92)90397-f"
}