Direct Binding of a Redox Protein for Single-Molecule Electron Transfer Measurements

被引：21

作者：

Della Pia, Eduardo A. ^{[1
,2
]}

Macdonald, J. Emyr ^{[1
,2
]}

Elliott, Martin ^{[1
,2
]}

Jones, D. Dafydd ^{[1
,2
]}

机构：

[1] Cardiff Univ, Sch Phys & Astron, Cardiff, S Glam, Wales

[2] Cardiff Univ, Sch Biosci, Cardiff, S Glam, Wales

来源：

SMALL | 2012年 / 8卷 / 15期

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

metalloproteins; molecular electronics; protein engineering; scanning probe microscopy; single-molecule studies; CYTOCHROME B(562); ESCHERICHIA-COLI; DNA-BINDING; TRANSPORT; GOLD; CONDUCTANCE;

D O I：

10.1002/smll.201102416

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

An electron transfer protein is engineered with two thiol groups introduced at different positions in the molecular structure to allow robust binding to two gold electrodes. Atomic force microscopy and scanning tunneling microscopy single-molecule studies show that the engineered proteins: (1) bind to a gold electrode in defined orientation dictated by the thiol-pair utilised, and (2) have a higher conductance than the wild-type proteins indicating a more efficient electron transmission due to the strong gold-thiol contacts. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：2341 / 2344

页数：4

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