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Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation

  • Lorena G. Fenoll , Francisco García-Molina , María A. Gilabert , Ramón Varón , Pedro A. García-Ruiz , José Tudela , Francisco García-Cánovas and José N. Rodríguez-López
Published/Copyright: July 5, 2005
Biological Chemistry
From the journal Volume 386 Issue 4

Abstract

The catalytic cycle of heme peroxidases involves three processes: the formation of compound I, its conversion to compound II and regeneration of the native enzyme. Each of the processes consists of a reversible binding stage followed by an irreversible transformation stage. Our group has proposed a continuous, sensitive and reliable chronometric method for measuring the steady-state rate of peroxidase activity. Furthermore, we have derived an analytical expression for the steady-state rate and simplified it, taking into consideration the experimental values of the rate constants of some stages previously determined by other authors in stopped-flow assays. We determined the value of the constant for the transformation of a series of phenols and anilines by compound II, and found that it involves a deprotonation step and an electron transfer step. Study of the solvent deuterium isotope effect on the oxidation of phenol revealed the non-rate-limiting character of the deprotonation step in a proton inventory study. Usage of the Marcus equation showed that the electronic transfer step is rate-limiting in both cases, while phenols and anilines were oxidised at different rates for the same potentials. This can be attributed to the shorter electron-tunnelling distance for electron transfer to the iron ion in the phenols than in the anilines.

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Published Online: 2005-07-05
Published in Print: 2005-04-01

© by Walter de Gruyter Berlin New York

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