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• W2108865938 abstract "The catalatic activity of chloroperoxidase (CPO) was demonstrated to exhibit saturation kinetics under steady-state conditions, which were not observed with catalase under comparable conditions. Results were obtained using reaction mixtures of CPO and H 2 O 2 at pH 6.2, rapid spectral scan and single wavelength measurements, and transient- and steady-state reaction conditions. The observed rectangular hyperbolae (measurement of rates of disappearance of H 2 O 2 and appearance of O 2 ) could be fit quantitatively to[Formula: see text]where v is rate of O 2 evolution, [CPO] 0 is total enzyme concentration, B 1 = (9 ± 1) × 10 2 s −1 , and B 2 = (3.3 ± 0.4) × 10 −3 M. The results indicated formation of a complex of compound I (CPO-I) and H 2 O 2 , which dissociated to native CPO, O 2 , and H 2 O with a rate constant of (9 ± 1) × 10 2 s −1 . The determination of the peroxidatic activity of CPO was performed using demethylation of N,N,N′,N′-tetramethyl-p-phenylenediamine (TMPD) under steady-state conditions. Attempts to determine Michaelis–Menten constants for the substrates TMPD and H 2 O 2 gave rise to apparently anomalous data. Our data showed that the modified ping–pong mechanism established for horseradish peroxidase is applicable to the peroxidatic reaction catalyzed by chloroperoxidase. Both peroxidatic and catalatic reactions occurred in the reaction system containing H 2 O 2 , a reducing substrate, and CPO. A combined reaction mechanism was proposed for CPO-catalyzed reactions in which the modified ping–pong mechanism was applicable for the peroxidatic reactions and the formation of a CPO-I–H 2 O 2 complex occurred for the catalatic reaction.Key words: chloroperoxidase, catalatic activity, peroxidatic activity, transient-state kinetics, steady-state kinetics." @default.
• W2108865938 created "2016-06-24" @default.
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• W2108865938 date "1994-07-01" @default.
• W2108865938 modified "2023-10-11" @default.
• W2108865938 title "Catalase activity of chloroperoxidase and its interaction with peroxidase activity" @default.
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• W2108865938 doi "https://doi.org/10.1139/o94-045" @default.
• W2108865938 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7893472" @default.
• W2108865938 hasPublicationYear "1994" @default.
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