Role of the reductant substrates on the inactivation of horseradish peroxidase by m-chloroperoxybenzoic acid.
Horseradish peroxidase reacts with H2O2 and other hydroperoxides to form Compound I, the first active enzymatic form m-Chloroperoxybenzoic acid, a xenobiotic hydroperoxide, acts as an oxidant substrate of horseradish peroxidase. However, this hydroperoxide is also a powerful inactivator of the enzyme and in this sense is more effective than H2O2. The coupled reductant substrates used in the peroxidatic reaction protect the enzyme from the inactivating process. A reaction mechanism is proposed with two competitive routes: one catalytic and one inactivating. Using a kinetic approach, the ratio between the hydroperoxide and the reductant substrate appears to be a decisive factor in the catalytic turnover of the enzyme. The role of the reductant substrates in protecting the enzyme, and the physiological and biotechnological implications of this process are discussed.
Arnao
M B
MB
Department of Plant Biology (Plant Physiology) and Department of Biochemistry and Molecular Biology-A-University of Murcia, Spain.
García-Cánovas
F
F
Acosta
M
M
D002723:Chlorobenzoates / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism*; D016877:Oxidants / Q000737:chemistry; D013057:Spectrum Analysis
D002723:Chlorobenzoates; D016877:Oxidants; D006735:Horseradish Peroxidase; C000433:3-chloroperbenzoic acid