@article{ref1,
title="tBOOH Acts as a Suicide Substrate for Catalase",
journal="Archives of biochemistry and biophysics",
year="1993",
author="Pichorner, H. and Jessner, G. and Ebermann, R.",
volume="300",
number="1",
pages="258-264",
abstract="The effects of t-butyl hydroperoxide (tBOOH) on bovine liver catalase were investigated. tBOOH is accepted as a substrate of catalase and in the absence of hydrogen donors leads to a destruction of the enzyme via compound II formation. During the decomposition of this enzyme-substrate complex catalase serves as internal hydrogen donor which results in destruction of the enzyme. Evidence for this destruction is given by: - a decrease of the Soret band in the uv/vis spectrum, - iron release from the enzyme, - decrease of the catalatic activity of the enzyme measured by oxygen release from hydrogen peroxide. Hydrogen donors like NADH and o-dianisidine have been found to protect the enzyme from destruction by tBOOH but lead to a structural alteration of the enzyme, shown by alteration of the electrophoretic mobility. In the presence of the hydrogen donor tBOOH is completely reduced to t-butanol, which is thought to proceed in a peroxidase-like reaction. © 1993 Academic Press, Inc.<p /><p>Language: en</p>",
language="en",
issn="0003-9861",
doi="10.1006/abbi.1993.1036",
url="http://dx.doi.org/10.1006/abbi.1993.1036"
}