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Temperature and Force Dependence of Nanoscale Electron Transport via the Cu Protein Azurin

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Department of Materials & Interfaces, Department of Organic Chemistry, Chemical Research Support, and §Department of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel
*Address correspondence to [email protected], [email protected]
Cite this: ACS Nano 2012, 6, 12, 10816–10824
Publication Date (Web):November 8, 2012
https://doi.org/10.1021/nn3041705
Copyright © 2012 American Chemical Society
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Abstract

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Solid-state electron transport (ETp) via a monolayer of immobilized azurin (Az) was examined by conducting probe atomic force microscopy (CP-AFM), as a function of both temperature (248–373K) and applied tip force (6–15 nN). At low forces, ETp via holo-Az (with Cu2+) is temperature-independent, but thermally activated via the Cu-depleted form of Az, apo-Az. While this observation agrees with those of macroscopic-scale measurements, we find that for holo-Az the mechanism of ETp at high temperatures changes upon an increase in the force applied by the tip to the proteins; namely, above 310 K and forces >6 nN ETp becomes thermally activated. This is in contrast to apo-Az, where increasing applied force causes only small monotonic increases in currents due to decreased electrode separation. The distinct ETp temperature dependence of holo- and apo-Az is assigned to a difference in structural response to pressure between the two protein forms. An important implication of these CP-AFM results (of measurements over a significant temperature range) is that for reliable ETp measurements on flexible macromolecules, such as proteins, the pressure applied during the measurements should be controlled or at least monitored.

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Additional information about AFM imaging, AFM tip scratching procedure, protein thickness measurements, and raw data of IV curves for Az and apo-Az at room temperature. This material is available free of charge via the Internet at http://pubs.acs.org.

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