Kinetic and stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide.
The inactivation of native chloroperoxidase (CPO) from Caldariomyces fumago in the presence of tert-butyl hydroperoxide (tert-BuOOH) was investigated. A kinetic analysis was made and the inactivation constants (V(3) and K(3)) were evaluated. In prolonged times, uni-exponential equation describes the enzyme time course inactivation. A method based on the rate of inactivation of the enzyme in the presence of the inactivating molecule tert-BuOOH was also performed. A second group of inactivation constants (j(3) and K) was obtained, which is sufficiently close to the first two, thus verifying that the decreasing of enzyme absorbance corresponds to the decay of activity.
Toti
Paolo
P
Unità di Biochimica, Dipartimento di Fisiologia e Biochimica, Università di Pisa, via S. Zeno 51, 56027 Pisa, Italy.
Petri
Antonella
A
Gambicorti
Tiziana
T
Osman
Ahmed M
AM
Bauer
Carlo
C
D001665:Binding Sites; D002711:Chloride Peroxidase / Q000187:drug effects / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004789:Enzyme Activation; D004795:Enzyme Stability / Q000187:drug effects; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology; D020122:tert-Butylhydroperoxide / Q000494:pharmacology*
D003577:Cytochrome P-450 Enzyme System; D020122:tert-Butylhydroperoxide; D002711:Chloride Peroxidase