Citation

Pichorner H, Jessner G, Ebermann R. Arch. Biochem. Biophys. 1993; 300(1): 258-264.

Copyright

(Copyright © 1993, Academic Press)

DOI

10.1006/abbi.1993.1036

PMID

unavailable

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.

Language: en