Premium
Direct Binding of a Redox Protein for Single‐Molecule Electron Transfer Measurements
Author(s) -
Della Pia Eduardo A.,
Macdonald J. Emyr,
Elliott Martin,
Jones D. Dafydd
Publication year - 2012
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201102416
Subject(s) - electron transfer , thiol , molecule , electrode , scanning tunneling microscope , redox , conductance , chemistry , nanotechnology , electron transport chain , quantum tunnelling , crystallography , materials science , inorganic chemistry , photochemistry , biochemistry , organic chemistry , optoelectronics , physics , condensed matter physics
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.