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Research article

Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2

Josefa HERNÁNDEZ-RUIZ, Marino B. ARNAO, Alexander N.P. HINER, Francisco GARCÍA-CÁNOVAS, Manuel ACOSTA
Biochemical Journal Feb 15, 2001, 354 (1) 107-114; DOI: 10.1042/bj3540107
Josefa HERNÁNDEZ-RUIZ
Departamento de Biología Vegetal (Fisiología Vegetal), Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
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Marino B. ARNAO
Departamento de Biología Vegetal (Fisiología Vegetal), Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
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Alexander N.P. HINER
Departamento de Biología Vegetal (Fisiología Vegetal), Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
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Francisco GARCÍA-CÁNOVAS
Departamento de Bioquímica y Biología Molecular-A, Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
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Manuel ACOSTA
Departamento de Biología Vegetal (Fisiología Vegetal), Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
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Abstract

H2O2 is the usual oxidizing substrate of horseradish peroxidase C (HRP-C). In the absence in the reaction medium of a one-electron donor substrate, H2O2 is able to act as both oxidizing and reducing substrate. However, under these conditions the enzyme also undergoes a progressive loss of activity. There are several pathways that maintain the activity of the enzyme by recovering the ferric form, one of which is the decomposition of H2O2 to molecular oxygen in a similar way to the action of catalase. This production of oxygen has been kinetically characterized with a Clark-type electrode coupled to an oxygraph. HRP-C exhibits a weak catalase-like activity, the initial reaction rate of which is hyperbolically dependent on the H2O2 concentration, with values for K2 (affinity of the first intermediate, compound I, for H2O2) and k3 (apparent rate constant controlling catalase activity) of 4.0±;0.6mM and 1.78±;0.12s-1 respectively. Oxygen production by HRP-C is favoured at pH values greater than approx. 6.5; under similar conditions HRP-C is also much less sensitive to inactivation during incubations with H2O2. We therefore suggest that this pathway is a major protective mechanism of HRP-C against such inactivation.

  • horseradish peroxidase C
  • oxygen
  • protection
  • The Biochemical Society, London © 2001
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February 2001

Volume: 354 Issue: 1

Biochemical Journal: 354 (1)
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Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2
Josefa HERNÁNDEZ-RUIZ, Marino B. ARNAO, Alexander N.P. HINER, Francisco GARCÍA-CÁNOVAS, Manuel ACOSTA
Biochemical Journal Feb 2001, 354 (1) 107-114; DOI: 10.1042/bj3540107
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Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2
Josefa HERNÁNDEZ-RUIZ, Marino B. ARNAO, Alexander N.P. HINER, Francisco GARCÍA-CÁNOVAS, Manuel ACOSTA
Biochemical Journal Feb 2001, 354 (1) 107-114; DOI: 10.1042/bj3540107

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Keywords

horseradish peroxidase C
oxygen
protection

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