Single-molecule mapping of long-range electron transport for a cytochrome b562 variant

Della Pia, Eduardo Antonio, Chi, Qijin, Jones, Darran Dafydd ORCID: https://orcid.org/0000-0001-7709-3995, Macdonald, John Emyr ORCID: https://orcid.org/0000-0001-5504-1692, Ulstrup, Jens and Elliott, Martin ORCID: https://orcid.org/0000-0002-9254-9898 2011. Single-molecule mapping of long-range electron transport for a cytochrome b562 variant. Nano Letters 11 (1) , pp. 176-182. 10.1021/nl103334q

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Abstract

Cytochrome b562 was engineered to introduce a cysteine residue at a surface-exposed position to facilitate direct self-assembly on a Au(111) surface. The confined protein exhibited reversible and fast electron exchange with a gold substrate over a distance of 20 Å between the heme redox center and the gold surface, a clear indication that a long-range electron-transfer pathway is established. Electrochemical scanning tunneling microscopy was used to map electron transport features of the protein at the single-molecule level. Tunneling resonance was directly imaged and apparent molecular conductance was measured, which both show strong redox-gated effects. This study has addressed the first case of heme proteins and offered new perspectives in single-molecule bioelectronics.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences Schools > Physics and Astronomy
Subjects:	Q Science > QC Physics Q Science > QD Chemistry
Uncontrolled Keywords:	Single-molecule electronics; Nanobioelectronics; Cytochrome b562; Protein engineering; Scanning tunneling microscopy; Redox-gated tunneling resonance
Publisher:	American Chemical Society
ISSN:	1530-6984
Last Modified:	17 Oct 2022 10:10
URI:	https://orca.cardiff.ac.uk/id/eprint/7282

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