Kinetic models of horseradish peroxidase action on a graphite electrode

Abstract The direct and mediated mechanisms of the electroreduction of hydrogen peroxide at a graphite electrode modified with horseradish peroxidase (HRP) were studied. The turnover number of the heterogeneous electron transfer between adsorbed HRP and the electrode was found to be equal to 0.66 ± 0.28 s −1 . The rate of the reaction of H 2 O 2 with HRP on the graphite surface was found to be 385 times slower than that in solution. p -Cresol, phenol and p -chlorophenol behaved as efficient mediators in the process of bioelectrochemical H 2 O 2 reduction. From the comparison of kinetically limited currents observed during direct and mediated reduction of H 2 O 2 it was concluded that the population of adsorbed HRP molecules and/or the graphite surface structure cannot be treated as homogeneous. It was found that 42% of the total amount of HRP molecules adsorbed on the electrode were accessible for direct unmediated electron transfer from the graphite electrode.

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