Oriented immobilization of a fully active monolayer of histidine-tagged recombinant laccase on modified gold electrodes

被引：72

作者：

Balland, Veronique ^{[1
]}

Hureau, Christelle ^{[1
]}

Cusano, Angela Maria ^{[2
]}

Liu, Yingli ^{[2
]}

Tron, Thierry ^{[2
]}

Limoges, Benoit ^{[1
]}

机构：

[1] Univ Paris Diderot, UMR CNRS 7591, Electrochim Mol Lab, F-75251 Paris 05, France

[2] Aix Marseille Univ Ctr Sci St Jerome, UMR CNRS 6263, Inst Sci Mol Marseille ISM2, F-13397 Marseille, France

来源：

CHEMISTRY-A EUROPEAN JOURNAL | 2008年 / 14卷 / 24期

关键词：

electrochemistry; enzymes; immobilization; redox mediators; self-assembled monolayers;

D O I：

10.1002/chem.200800368

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The formation of a dense monolayer of histidine-tagged recombinant laccase on gold electrodes by using a short thiol-NTA linker is described, as well as a kinetic analysis of the process by cyclic voltammetry. From a detailed analysis of the catalytic reduction of dioxygen by laccase in the presence of a one-electron redox mediator it can be concluded that the immobilized enzyme remains as active as in homogeneous solution.

引用

页码：7186 / 7192

页数：7

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