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PublicationBiosensors & Bioelectronics
Year2008
Volume24
Pages531-537
International

Laccase electrode for direct electrocatalytic reduction of O2 to H2O with high-operational stability and resistance to chloride inhibition

Authors:Cristina Vaz Dominguez, Susana Campuzano , Olaf Rüdiger , Marcos Pita Martínez, Marina Gorbacheva , Sergey Shleev , Víctor Manuel Fernández López, Antonio López de Lacey
Groups of research:BioElectroCatalysis
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/cm2 of electrocatalytic reduction of O2 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, O2 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 O2. Thus, two different modes of laccase inhibition by halides are discussed.
Keywords:Laccase; Cathode; Biofuel cells; Direct electron transfer
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