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

Eduardo Antonio Della Pia, Qijin Chi, D. Dafydd Jones, J. Emyr Macdonald, Jens Ulstrup, Martin Elliott

Research output: Contribution to journalJournal articleResearchpeer-review


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
Pages (from-to)176-182
Publication statusPublished - 2011


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


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