期刊
JOURNAL OF PHYSICAL CHEMISTRY C
卷 116, 期 31, 页码 16532-16540出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp303818p
关键词
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资金
- DGI (Ministerio de Ciencia e Innovacion) [CTQ2009-07017, CTQ2009-12649]
- European Union [NMP4-SL-2009-229255]
- JAE-Doc fellowship from CSIC
- Spanish MICINN
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) x 10(11) laccase units per cm(2) 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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