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Irreversible inactivation of Caldariomyces fumago chloroperoxidase by hydrogen peroxide
Author(s) -
Shevelkova Angeli.,
Ryabov Alexander D.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201731
Subject(s) - chemistry , hydrogen peroxide , bromide , halogenation , peroxidase , horseradish peroxidase , chloride , inorganic chemistry , reaction rate constant , medicinal chemistry , photochemistry , enzyme , kinetics , organic chemistry , physics , quantum mechanics
The rate constants for the H2O2‐induced irreversible inactivation (kinact) of chloroperoxidase from Caldariomyces fumago evaluated from the analysis of complete kinetic curves of chlorination or bromination of monochlorodimedon were found to follow the rate law kinact = k[H2O2]/(K + [H2O2]) with k = 0.009±0.002 and 0.0095±0.0010 s‐1 and K = (13±4)×10‐3 and (9±2)×10‐3 M in the presence of 0.01 M chloride and bromide, respectively, at pH 2.75 and 25 °C. The data show that chloroperoxidase investigated is more than by a factor of 10 less resistant toward hydrogen peroxide compared to horseradish peroxidase. The possible reason for it and the biotechological implications are briefly discussed.