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RevistaJournal of Physical Chemistry C
Año2012
Volumen116
Páginas16532−16540
Internacional

Combined ATR-SEIRAS and EC-STM Study of the Immobilization of Laccase on Chemically Modified Au Electrodes

Autores:Cristina Vaz Dominguez, Marcos Pita Martínez, Antonio López de Lacey, Sergey Shleev , Ángel Cuesta Ciscar
Grupos de investigación:BioElectroCatálisis

The successive steps of laccase immobilization on chemically

modified Au electrodes were monitored using ATR-SEIRAS and in

situ STM. Successful covalent immobilization of the enzyme on Au

electrodes modified by a mixed aminophenyl-mercaptohexanol adlayer and

on Au electrodes modified by a 4-aminothiophenyl SAM via a Schiff base

reaction followed by the formation of amide bonds is revealed by the

emergence of the corresponding bands in the ATR-SEIRA spectra, and an

enzyme coverage on aminophenyl-mercaptohexanol-modified Au electrodes

of about (7.27 ± 1.93) °— 1011 laccase units per cm2 was calculated

from STM images. The small differences between the ATR-SEIRA spectra

of the enzyme immobilized on aminophenyl-mercaptohexanol-modified

Au electrodes and the ATR-SEIRA spectra of the enzyme immobilized on

4-aminothiophenyl-modified Au electrodes are attributed to a different

orientation of the immobilized enzyme due to the presence on the surface of aminophenyl-mercaptohexanol-modified Au

electrodes of OH functional groups that favor an orientation of laccase with the Cu T1 center of the enzyme facing the electrode

surface, thus, allowing a high activity for direct electrocatalysis of the ORR at low overpotentials.

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