Publication: Research - peer-review › Journal article – Annual report year: 2011
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.
|Citations||Web of Science® Times Cited: 28|
- Redox-gated tunneling resonance, Cytochrome b562, Protein engineering, Single-molecule electronics, Scanning tunneling microscopy, Nanobioelectronics