Catalase catalyzes of peroxynitrite-mediated phenolic nitration.
Catalase catalyzed the peroxynitrite-mediated nitration of 4-hydroxyphenylacetic acid. The curve for the pH dependence of nitration was similar to that for the reaction between peroxynitrite and phenol. Cyanide, azide, and 3-amino-1,2,4-triazole inhibited the nitration in a dose-dependent way. When catalase was mixed with peroxynitrite, Compound I was detected as an intermediate. Because azide was an electron donor for the peroxidatic action of catalase, and because 3-amino-1,2,4-triazole inhibited catalase activity by binding with Compound I, peroxynitrite-mediated phenolic nitration was probably accompanied by Compound I formation. Both catalase and superoxide dismutase protected Escherichia coli from peroxynitrite toxicity.
Kono
Y
Y
Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Japan. ykono@life.shimane-u.ac.jp
Yamasaki
T
T
Ueda
A
A
Shibata
H
H
D000818:Animals; D002374:Catalase / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D004926:Escherichia coli / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D009566:Nitrates / Q000378:metabolism* / Q000494:pharmacology; D016877:Oxidants / Q000378:metabolism* / Q000494:pharmacology; D010648:Phenylacetates / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000378:metabolism
D009566:Nitrates; D016877:Oxidants; D010648:Phenylacetates; C039642:peroxynitric acid; C008070:4-hydroxyphenylacetic acid; D002374:Catalase; D013482:Superoxide Dismutase