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PublicationJournal of Physical Chemistry CThe 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.
Year2012
Volume116
Pages16532−16540
International

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

Authors:Cristina Vaz Dominguez, Marcos Pita Martínez, Antonio López de Lacey, Sergey Shleev , Ángel Cuesta Ciscar
Groups of research:BioElectroCatalysis

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.

Keywords:
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