Journal
BIOSENSORS & BIOELECTRONICS
Volume 24, Issue 4, Pages 531-537Publisher
ELSEVIER ADVANCED TECHNOLOGY
DOI: 10.1016/j.bios.2008.05.002
Keywords
Laccase; Cathode; Biofuel cells; Direct electron transfer
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Funding
- Spanish Ministerio de Educacion y Ciencia [CTQ2006-12097]
- Swedish Research Council [621-2005-3581]
- Ministerio de Educacion y Ciencia
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Laccase from Trametes hirsuta basidiomycete has been covalently bound to graphite electrodes electrochemically modified with phenyl derivatives as a way to attach the enzyme molecules with an adequate orientation for direct electron transfer(DET). Current densities up to 0.5 mA/cm(2) of electrocatalytic reduction of O-2 to H2O were obtained in absence of redox mediators, suggesting preferential orientation of the T1 Cu centre of the laccase towards the electrode. The covalent attachment of the laccase molecules to the functionalized electrodes permitted remarkable operational stability. Moreover, O-2 bioelectroreduction based on DET between the laccase and the electrode was not inhibited by chloride ions, whereas mediated bioelectrocatalysis was. In contrast, fluoride ions inhibited both direct and mediated electron transfers-based bioelectrocatalytic reduction of O-2. Thus, two different modes of laccase inhibition by halides are discussed. (C) 2008 Elsevier B.V. All rights reserved.
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