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

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

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Publication Article, peer reviewed scientific
Title Laccase electrode for direct electrocatalytic reduction of O2 to H2O with high-operational stability and resistance to chloride inhibition.
Author(s) Vaz-Dominguez, Cristina ; Campuzano, Susana ; Ruediger, Olaf ; Pita, Marcos ; Gorbacheva, Marina ; Shleev, Sergey ; Fernandez, Victor ; De Lacey, Antonio
Date 2008
English abstract
Laccase from Trametes hirsuta basidiomycete has been covalently bound to graphite electrodes electrochem. modified with Ph derivs. as a way to attach the enzyme mols. with an adequate orientation for direct electron transfer (DET). Current densities up to 0.5 mA/cm2 of electrocatalytic redn. of O2 to H2O were obtained in absence of redox mediators, suggesting preferential orientation of the T1 Cu center of the laccase towards the electrode. The covalent attachment of the laccase mols. to the functionalized electrodes permitted remarkable operational stability. Moreover, O2 bioelectroredn. 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 redn. of O2. Thus, two different modes of laccase inhibition by halides are discussed.
DOI http://dx.doi.org/10.1016/j.bios.2008.05.002 (link to publisher's fulltext.)
Publisher Elsevier
Host/Issue Biosensors & Bioelectronics
Volume 24
ISSN 0956-5663
Pages 531-537
Language eng (iso)
Subject(s) Laccase, Cathode, Biofuel cell
Medicine
Research Subject Categories::MEDICINE::Chemistry::Biochemistry
Handle http://hdl.handle.net/2043/6875 (link to this page)

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