title: Direct binding of a redox protein for single-molecule electron transfer measurements.
abstract: 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.
authors.affiliation: School of Physics and Astronomy and School of Biosciences, Cardiff University, Cardiff, UK.
authors.forename: Eduardo A
authors.initials: EA
authors.lastname: Della Pia
authors.forename: J Emyr
authors.initials: JE
authors.lastname: Macdonald
authors.forename: Martin
authors.initials: M
authors.lastname: Elliott
authors.forename: D Dafydd
authors.initials: DD
authors.lastname: Jones
mesh_terms: D004563:Electrochemistry; D004579:Electron Transport / Q000502:physiology*; D008667:Metalloproteins / Q000737:chemistry; D016252:Microscopy, Scanning Tunneling; D036103:Nanotechnology / Q000379:methods*; D010084:Oxidation-Reduction; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry*
chemical_list: D008667:Metalloproteins; D011506:Proteins