PMID: 9165102Apr 25, 1997Paper

Kinetic studies on the oxidation of phenols by the horseradish peroxidase compound II

Biochimica Et Biophysica Acta
P K PatelD V Behere

Abstract

Oxidation of substituted phenols by horseradish peroxidase compound II were studied using stopped-flow technique. Dissociation constants (K(D)) of HRP-II-phenol complexes were deduced from the kinetic data. Magnitudes of K(D) fall in a relatively narrow range of 3-11 mM. These are comparable to 3-10 mM reported for the binding of substituted phenols to native HRP, suggesting that the mode of binding of phenols to native HRP and HRP compound II may be similar. pH dependence of the apparent second order rate constants (k(app)) of the reactions of all the phenols were determined. The k(app) values of reactions other than the reaction of tyrosine, were observed to increase in the acidic region but decreased in the alkaline region. The increase was attributed to the deprotonation of distal carboxylic acid residue on enzyme with pK(a) values of 4.2-5.2. For tyrosine, however, the apparent second-order rate constant was observed to further increase non linearly on increasing the pH in the alkaline region. Results were interpreted quantitatively on the basis that protonated form of the enzyme reacted with the protonated form of the phenol with different individual rate constants.

Citations

Apr 14, 2006·Bioprocess and Biosystems Engineering·R H CarvalhoJ M S Cabral
Sep 30, 1994·Journal of Biotechnology·E Bartonek-Roxå, H Eriksson
Mar 27, 2003·Chemosphere·Jiasong Fang, Michael J Barcelona
Dec 22, 2006·Biochimica Et Biophysica Acta·Stefan FranzenJennifer L Belyea
Jan 18, 2005·Biological Chemistry·M Angeles GilabertJosé N Rodríguez-López
Apr 4, 2014·Chemical Reviews·Luisa B Maia, José J G Moura
Jul 25, 2000·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·J KulysA Ziemys
Jan 12, 2007·The Journal of Physical Chemistry. B·Rafael AndreuJuan Jose Calvente

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