English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/163747
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Direct heterogeneous electron transfer reactions of fungal laccases at bare and thiol-modified gold electrodes

AuthorsPita, Marcos ; Shleev, Sergey; Ruzgas, Tautgirdas; Fernández López, Víctor Manuel ; Yaropolov, Alexander I.; Gorton, Lo
Redox potential
T1, T2, and T3 sites
Gold electrode
Cyclic voltammetry
Issue DateMay-2006
CitationElectrochemistry Communications 8(5): 747-753 (2006)
AbstractMediatorless (direct) electron transfer between bare and thiol-modified gold electrodes and fungal laccases from different sources has been demonstrated. The electrochemical activity of the enzymes from basidiomycetes Trametes hirsuta, Trametes ochracea, and Cerrena maxima under aerobic and anaerobic conditions can clearly be observed using cyclic voltammetry and spectroelectrochemistry. Bioelectroreduction of oxygen by T. hirsuta laccase immobilized on amino-thiophenol-modified gold electrodes, starting at +625 mV vs. NHE, is demonstrated and differences in bioelectrocatalysis of the enzyme immobilized on bare and thiol-modified electrodes are shown. It was found that hydrogen peroxide was one of the products of oxygen electroreduction on gold electrodes modified with fungal laccases, whereas no significant peroxide formation was observed for T. hirsuta laccase immobilised on thiol-modified gold electrodes. Thus, a hypothesis about two different mechanisms of oxygen electroreduction by fungal laccases adsorbed on bare and thiol-modified electrodes is proposed.
Publisher version (URL)https://doi.org/10.1016/j.elecom.2006.03.008
Appears in Collections:(ICP) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.