Puede utilizar el filtro de búsqueda del panel izquierdo para acotar los resultados
Tipo de publicación
Todos Libros Revistas
Palabras clave
Acceso DOI
Acceso digital CSIC
Datos técnicos
RevistaJournal of Physical Chemistry C

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:BioElectroCatalisis

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.

Palabras clave:
logo de CSIC