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Eduardo A. Della Pia, J. Emyr Macdonald, Martin Elliott and D. Dafydd Jones Direct Binding of a Redox Protein for Single-Molecule Electron Transfer Measurements Small 8

Version of Record online: 2 MAY 2012 | DOI: 10.1002/smll.201102416

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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.

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