TY - JOUR
T1 - Electronic Conductance Resonance in Non-Redox-Active Proteins
AU - Zhang, Bintian
AU - Song, Weisi
AU - Brown, Jesse
AU - Nemanich, Robert
AU - Lindsay, Stuart
N1 - Funding Information:
This work was supported by grants HG006323 and HG010522 from the National Human Genome Research Institute, Recognition AnalytiX Corp., and the Edward and Nadine Carson Endowment.
Publisher Copyright:
Copyright © 2020 American Chemical Society.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - Bioelectronics research has mainly focused on redox-active proteins because of their role in biological charge transport. In these proteins, electronic conductance is a maximum when electrons are injected at the known redox potential of the protein. It has been shown recently that many non-redox-active proteins are good electronic conductors, though the mechanism of conduction is not yet understood. Here, we report single-molecule measurements of the conductance of three non-redox-active proteins, maintained under potential control in solution, as a function of electron injection energy. All three proteins show a conductance resonance at a potential âˆ0.7 V removed from the nearest oxidation potential of their constituent amino acids. If this shift reflects a reduction of reorganization energy in the interior of the protein, it would account for the long-range conductance observed when carriers are injected into the interior of a protein.
AB - Bioelectronics research has mainly focused on redox-active proteins because of their role in biological charge transport. In these proteins, electronic conductance is a maximum when electrons are injected at the known redox potential of the protein. It has been shown recently that many non-redox-active proteins are good electronic conductors, though the mechanism of conduction is not yet understood. Here, we report single-molecule measurements of the conductance of three non-redox-active proteins, maintained under potential control in solution, as a function of electron injection energy. All three proteins show a conductance resonance at a potential âˆ0.7 V removed from the nearest oxidation potential of their constituent amino acids. If this shift reflects a reduction of reorganization energy in the interior of the protein, it would account for the long-range conductance observed when carriers are injected into the interior of a protein.
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U2 - 10.1021/jacs.0c01805
DO - 10.1021/jacs.0c01805
M3 - Article
C2 - 32176496
AN - SCOPUS:85083647101
SN - 0002-7863
VL - 142
SP - 6432
EP - 6438
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 13
ER -