Orientation-dependent electron transport in a single redox protein [RETRACTED]

Della Pia, Eduardo Antonio, Elliott, Martin ORCID: https://orcid.org/0000-0002-9254-9898, Jones, Darran Dafydd ORCID: https://orcid.org/0000-0001-7709-3995 and Macdonald, J. Emyr ORCID: https://orcid.org/0000-0001-5504-1692 2012. Orientation-dependent electron transport in a single redox protein [RETRACTED]. ACS Nano 6 (1) , pp. 355-361. 10.1021/nn2036818

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Abstract

The redox-active protein cytochrome b562 has been engineered to introduce pairs of thiol groups in the form of cysteine residues at specified sites. Successful STM imaging of the molecules adsorbed on a gold surface indicated that one thiol group controls the orientation of the molecule and that the protein maintains its native form under the experimental conditions. Stable protein–gold STM tip electrical contact was directly observed to form via the second free thiol group in current–voltage and current–distance measurements. Proteins with thiol contacts positioned across the protein’s short axis displayed a conductance of (3.48 ± 0.05) × 10–5G0. However proteins with thiol groups placed along the long axis reproducibly yielded two distinct values of (1.95 ± 0.03) × 10–5G0 and (3.57 ± 0.11) × 10–5G0, suggesting that the placement of the asymmetrically located haem within the protein influences electron transfer. In contrast, the unengineered wild-type cytochrome b562 had conductance values at least 1 order of magnitude less. Here we show that an electron transfer protein engineered to bind gold surfaces can be controllably oriented and electrically contacted to metallic electrodes, a prerequisite for potential integration into electronic circuits.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Physics and Astronomy Biosciences
Subjects:	Q Science > QC Physics
Uncontrolled Keywords:	single-molecule conductance; molecular electronics; nanobioelectronics; scanning tunneling microscopy; cytochrome b562; protein engineering
Additional Information:	This article has been retracted. Please follow the links to the journal website for more information. Notice DOI: 10.1021/acsnano.6b06727
Publisher:	American Chemical Society
ISSN:	1936-0851
Last Modified:	19 Oct 2022 08:50
URI:	https://orca.cardiff.ac.uk/id/eprint/19243

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