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Electroenzymatic reactions with oxygen on laccase-modified electrodes in anhydrous (pure) organic solvent

Author

Summary, in English

The electroenzymatic reactions of Trametes hirsuta laccase in the pure organic solvent dimethyl sulfoxide (DMSO) have been investigated within the framework for potential use as a catalytic reaction scheme for oxygen reduction. The bioelectrochemical characteristics of laccase were investigated in two different ways: (i) by studying the electroreduction of oxygen in anhydrous DMSO via a direct electron transfer mechanism without proton donors and (ii) by doing the same experiments in the presence of laccase substrates, which display in pure organic solvents both the properties of electron donors as well as the properties of weak acids. The results obtained with laccase in anhydrous DMSO were compared with those obtained previously in aqueous buffer. It was shown that in the absence of proton donors under oxygenated conditions, formation of superoxide anion radicals is prevented at bare glassy carbon and graphite electrodes with adsorbed laccase. The influence of the time for drying the laccase solution at the electrode surface on the electroreduction of oxygen was studied. Investigating the electroenzymatic oxidation reaction of catechol and hydroquinone in DMSO reveals the formation of various intermediates of the substrates with different electrochemical activity under oxygenated conditions. The influence of the content of aqueous buffer in the organic solvent on the electrochemical behaviour of hydroquinone/1,4-benzoquinone couple was also studied. (C) 2006 Elsevier B.V. All fights reserved.

Publishing year

2007

Language

English

Pages

199-204

Publication/Series

Bioelectrochemistry

Volume

70

Issue

2

Document type

Journal article

Publisher

Elsevier

Topic

  • Analytical Chemistry

Keywords

  • anhydrous organic solvent
  • laccase
  • electroenzymatic reaction
  • dimethyl
  • sulfoxide

Status

Published

ISBN/ISSN/Other

  • ISSN: 1878-562X