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Direct electron transfer of multicopper oxidases to electrodes via their Cu T1 site for biofuel cell applications

AuthorsLópez de Lacey, Antonio ; Gutiérrez Sánchez, Cristina ; Pita, Marcos ; Shleev, Sergey
Issue DateSep-2012
Citation11th European Biological Inorganic Chemistry Conference (2012)
AbstractLaccases and bilirubin oxidases are Cu metalloenzymes that catalyze the direct reduction of O2 to H2O. These enzymes are the best candidates for enzymatic biofuel cell cathodes due to their efficient catalytic properties. These types of redox enzymes are suitable for direct electron transfer electrodes when appropriately wired toward different electroactive surfaces such as gold or graphite. In our group we have developed several of these strategies by covalent and oriented immobilization of both types of metalloenzymes with their Cu-T1 site facing the electrode surface. This metal ion is the redox site that accepts the 4 electrons from the donor that are required to reduce O2 to H2O in the T2-T3 site, which is formed by the other 3 Cu of the metalloenzymes. Fungal laccases have the advantage of catalyzing oxygen reduction at higher redox potential for biofuel cell applications. On the other hand, laccases suffer several hindering conditions when working in many in vivo-like environments, being the most relevant chloride inhibition and the neutral pH. This presentation will show strategies to improve laccase performance under these non-favoured environments. We have shown that specific orientation of laccase for DET can reduce this inhibition source when immobilized on a low-density graphite (LDG) electrode, and how to extend this immobilization method to gold planar electrodes. We will show the improvement brought to current density and chloride resistance by combining a LDG electrode with gold nanoparticles. The limitations brought by the use of neutral pH can be addressed by generation of a local acidic pH environment due to co-immobilization of a second enzyme (glucose oxidase). In addition, results of electrocatalytic performance of immobilized bilirubin oxidase in “blood-mimic” buffer will be shown.
DescriptionTrabajo presentado en la 11th European Biological Inorganic Chemistry Conference (EUROBIC11), celebrada en Granada del 12 al 16 de septiembre de 2012.
Appears in Collections:(ICP) Comunicaciones congresos
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