Direct binding of a redox protein for single-molecule electron transfer measurements

Della Pia, Eduardo Antonio, Macdonald, John Emyr ORCID: https://orcid.org/0000-0001-5504-1692, Elliott, Martin ORCID: https://orcid.org/0000-0002-9254-9898 and Jones, Darran Dafydd ORCID: https://orcid.org/0000-0001-7709-3995 2012. Direct binding of a redox protein for single-molecule electron transfer measurements. Small 8 (15) , pp. 2341-2344. 10.1002/smll.201102416

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Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences Physics and Astronomy
Subjects:	Q Science > QC Physics Q Science > QD Chemistry
Uncontrolled Keywords:	metalloproteins; molecular electronics; protein engineering; scanning probe microscopy; single-molecule studies
Publisher:	Wiley-Blackwell
ISSN:	1613-6810
Last Modified:	10 Apr 2023 06:21
URI:	https://orca.cardiff.ac.uk/id/eprint/46607

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