Direct electrochemistry of horseradish peroxidase immobilized in a chitosan–[C4mim][BF4] film: Determination of electrode kinetic parameters

Long, Jenny S., Silvester, Debbie S., Wildgoose, Gregory, Surkus, Annette-E., Flechsig, Gerd-Uwe and Compton, Richard G. (2008) Direct electrochemistry of horseradish peroxidase immobilized in a chitosan–[C4mim][BF4] film: Determination of electrode kinetic parameters. Bioelectrochemistry, 74 (1). pp. 183-187. ISSN 1878-562X

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Abstract

The direct electrochemistry of a HRP–chi–[C4mim][BF4] film (where HRP = horseradish peroxidase, chi = chitosan, and [C4mim][BF4] = the room temperature ionic liquid (RTIL) 1-butyl-3-methylimidazolium tetrafluoroborate) has been studied by cyclic voltammetry on a glassy carbon electrode. The mechanism for the electrochemical reaction of HRP is suggested to be EC for the reduction, and CE for the following re-oxidation, as the oxidative peak potential remained approximately unchanged across the scan rate range. The half wave potential of HRP reduction was found to be pH dependent, suggesting that a concomitant proton and electron transfer is occurring. Using theoretical simulations of the experimentally obtained peak positions, the standard electron transfer rate constant, k0, was found to be 98 (± 16) s- 1 at 295 K in pH 7 phosphate buffer solution, which is very close to the value reported in the absence of ionic liquid. This suggests that the ionic liquid used here in the HRP–chi–[C4mim][BF4]/GC electrode does not enhance the rate of electron transfer. k0 was found to increase systematically with increasing temperature and followed a linear Arrhenius relation, giving an activation energy of 14.20 kJ mol- 1. The electrode kinetics and activation energies obtained are identical to those reported for HRP films in aqueous media. This leads us to question if the use of RTIL films provide any unique benefits for enzyme/protein voltammetry. Rather the films may likely contain aqueous zones in which the enzymes are located and undergo electron transfer.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Depositing User: Rachel Smith
Date Deposited: 29 Mar 2011 16:20
Last Modified: 02 Sep 2019 14:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/27485
DOI: 10.1016/j.bioelechem.2008.07.008

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