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Kinetics of phenol oxidation by peroxidase

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Abstract

Studies of the kinetic behavior of horseradish peroxidase (HRP) at pH 8 and at room temperature indicate that the reaction of phenol with H2O2 catalyzed by HRP exhibits normal Michaelis-Menten saturation kinetics. An irreversible reaction mechanism for the steady-state kinetics of HRP, which is consistent with the experimental data, is considered. The second-order rate constants for the reactions of HRP with H2O2 and compound II with phenol are 4.14 × 105 M-1s-1 and 5.54 × 104M-1s-1, respectively.

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Abbreviations

•AH:

Free radical

AH2 :

Phenol or aromatic compound

Compound I:

Intermediate oxidized enzymatic form of horseradish peroxidase by H2O2

Compound II:

Intermediate oxidized enzymatic form of Compound I by phenol

Etot :

Total native enzyme horseradish peroxidase

HRP:

Native enzyme horseradish peroxidase

k1 :

Rate constant for Compound I formation

k-1 :

Rate constant for Compound I back to the native enzyme

k2 :

Rate constant for one-electron reduction of Compound I by phenol

k3 :

Rate constant for one-electron reduction of Compound II by phenol

Km′ :

Apparent Michaelis constant at constant phenol concentration, mM

Km′’ :

Apparent Michaelis constant at constant H2O2 concentration, mM

V :

Initial reaction rate, mM/s

Vmax′ :

Apparent maximum reaction rate at constant phenol concentration, mM/s

Vmax′’:

Apparent maximum reaction rate at constant H2O2 concentration, mM/s

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Authors and Affiliations

  1. Department of Chemical Engineering, Kingsbury Hall, University of New Hampshire, 03824, Durham, NH

    Palligarnai T. Vasudevan & Luting Olivia Li

Authors
  1. Palligarnai T. Vasudevan
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  2. Luting Olivia Li
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Vasudevan, P.T., Li, L.O. Kinetics of phenol oxidation by peroxidase. Appl Biochem Biotechnol 60, 203–215 (1996). https://doi.org/10.1007/BF02783584

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  • DOI: https://doi.org/10.1007/BF02783584

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