@article{ref1,
title="A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide",
journal="Biochimica et biophysica acta",
year="1990",
author="Arnao, M. B. and Acosta, M. and del Río, J. A. and Varon, R. and García-Cánovas, F.",
volume="1041",
number="1",
pages="43-47",
abstract="In the absence of reductant substrates, and with excess H2O2, peroxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) shows the kinetic behaviour of a suicide inactivation, H2O2 being the suicide substrate. From the complex (compound I-H2O2), a competition is established between two catalytic pathways (the catalase pathway and the compound III-forming pathway), and the suicide inactivation pathway (formation of inactive enzyme). A kinetic analysis of this system allows us to obtain a value for the inactivation constant, ki = (3.92 +/- 0.06) x 10(-3) x s-1. Two partition ratios (r), defined as the number of turnovers given by one mol of enzyme before its inactivation, can be calculated: (a) one for the catalase pathway, rc = 449 +/- 47; (b) the other for the compound III-forming pathway, rCoIII = 2.00 +/- 0.07. Thus, the catalase activity of the enzyme and, also, the protective role of compound III against an H2O2-dependent peroxidase inactivation are both shown to be important.<p /><p>Language: en</p>",
language="en",
issn="0006-3002",
doi="10.1016/0167-4838(90)90120-5",
url="http://dx.doi.org/10.1016/0167-4838(90)90120-5"
}