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Communication
Direct Binding of a Redox Protein for Single-Molecule Electron Transfer Measurements
Article first published online: 2 MAY 2012
DOI: 10.1002/smll.201102416
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Della Pia, E. A., Macdonald, J. E., Elliott, M. and Jones, D. D. (2012), Direct Binding of a Redox Protein for Single-Molecule Electron Transfer Measurements. Small, 8: 2341–2344. doi: 10.1002/smll.201102416
Publication History
- Issue published online: 1 AUG 2012
- Article first published online: 2 MAY 2012
- Manuscript Revised: 16 FEB 2012
- Manuscript Received: 17 NOV 2011
Keywords:
- metalloproteins;
- molecular electronics;
- protein engineering;
- scanning probe microscopy;
- single-molecule studies
An electron transfer protein is engineered with two thiol groups introduced at different positions in the molecular structure to allow robust binding to two gold electrodes. Atomic force microscopy and scanning tunneling microscopy single-molecule studies show that the engineered proteins: (1) bind to a gold electrode in defined orientation dictated by the thiol-pair utilised, and (2) have a higher conductance than the wild-type proteins indicating a more efficient electron transmission due to the strong gold–thiol contacts.