期刊
NANOSCALE
卷 10, 期 46, 页码 21712-21720出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8nr06627b
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资金
- Israel Science Foundation
- Minerva Foundation (Munich)
- Nancy and Stephen Grand Center for Sensors and Security
- Benoziyo Endowment Fund for the Advancement of Science and J & R Center for Scientific Research
- Kimmelman Center for Biomolecular Structure and Assembly
The incorporation of proteins as functional components in electronic junctions has received much interest recently due to their diverse bio-chemical and physical properties. However, information regarding the energies of the frontier orbitals involved in their electron transport (ETp) has remained elusive. Here we employ a new method to quantitatively determine the energy position of the molecular orbital, nearest to the Fermi level (E-F) of the electrode, in the electron transfer protein Azurin. The importance of the Cu(ii) redox center of Azurin is demonstrated by measuring gate-controlled conductance switching which is absent if Azurin's copper ions are removed. Comparing different electrode materials, a higher conductance and a lower gate-induced current onset is observed for the material with smaller work function, indicating that ETp via Azurin is LUMO-mediated. We use the difference in work function to calibrate the difference in gate-induced current onset for the two electrode materials, to a specific energy level shift and find that ETp via Azurin is near resonance. Our results provide a basis for mapping and studying the role of energy level positions in (bio)molecular junctions.
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