Single-molecule Mapping of Long-range Electron Transfer for a Cytochrome b562 Variant

Publication: Research - peer-reviewJournal article – Annual report year: 2011

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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.
Original languageEnglish
JournalNano Letters
Publication date2011
Volume11
Pages176-182
ISSN1530-6984
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 20

Keywords

  • Redox-gated tunneling resonance, Cytochrome b562, Protein engineering, Single-molecule electronics, Scanning tunneling microscopy, Nanobioelectronics
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