Conductive atomic force microscopy study of plastocyanin molecules adsorbed on gold electrode

被引:29
作者
Andolfi, L [1 ]
Cannistraro, S [1 ]
机构
[1] Univ Tuscia, Dipartimento Sci Ambientali, INFM, CNISM,Biophys & Nanosci Ctr, I-01100 Viterbo, Italy
关键词
metalloprotein; conduction; plastocyanin; conductive atomic force microscopy;
D O I
10.1016/j.susc.2005.08.027
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The electrical conduction of mutant plastocyanin molecules self-assembled on gold was measured by conductive atomic force microscopy. The copper protein molecules, able to bind to gold through an engineered S-S group, were immobilised on Au(111) substrates to form a dense monolayer, which was contacted by a conductive atomic force microscopy tip at controlled force. Specifically, the electronic conduction of the gold coated tip-plastocyanin-Au(111) junction was well characterised between +1 and -1 V for increasing compressional forces. The conduction varies slightly within the force range of 3-9 nN, while it rapidly increases above these force values. The occurrence of a jump in mutant plastocyanin conduction at a critical force value, suggests that the current transport mechanism through the bioelectronic junction can be dominated by protein mechanical characteristics and/or by considerable variations in the protein conduction upon molecular deformation. By operating in imaging mode, we have obtained good topographic images of the protein self-assembled on Au(111) surface and for the first time simultaneous current images were recorded. Remarkably, a correspondence between the biomolecules observed in the topography images and the current spots was found for negative bias. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:68 / 77
页数:10
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