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Evaluating Plasmonic Transport in Current-carrying Silver Nanowires
Published on: December 11, 2013
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Structural basis for metallic-like conductivity in microbial nanowires
Nikhil S Malvankar, Madeline Vargas, Kelly Nevin1
1Department of Microbiology, University of Massachusetts, Amherst, Massachusetts, USA.
Mbio
|March 5, 2015
Summary
Geobacter sulfurreducens pili exhibit metallic-like conductivity due to aromatic amino acids. Structural analysis revealed a 3.2-Å spacing linked to this conductivity, supporting their role as electronically functional proteins.
Area of Science:
- Microbiology
- Biophysics
- Materials Science
Background:
- Geobacter sulfurreducens pili, known as microbial nanowires, facilitate long-range electron transport.
- These pili exhibit metallic-like conductivity, a rare property for proteins, with implications for biogeochemical cycling and bioelectronics.
- Previous homology models conflicted with experimental conductivity data.
Purpose of the Study:
- To investigate the structural basis for the metallic-like conductivity of Geobacter sulfurreducens pili.
- To resolve discrepancies between structural predictions and measured conductivity.
- To provide insights for designing novel bioelectronic materials.
Main Methods:
- Synchrotron X-ray microdiffraction and rocking-curve X-ray diffraction were employed.
- Pili from wild-type and nonconductive mutant strains (Aro5) were analyzed.
- Structural analysis was correlated with pH-dependent conductivity measurements.
Main Results:
- A periodic 3.2-Å spacing was identified in conductive pili, absent in nonconductive pili lacking aromatic amino acids.
- The intensity of the 3.2-Å peak showed a 100-fold increase with a pH shift that also increased conductivity 100-fold.
- A revised homology model predicted aromatic amino acid packing consistent with experimental findings.
Conclusions:
- The 3.2-Å spacing, attributed to overlapping π-orbitals of aromatic amino acids, is crucial for metallic-like conductivity.
- Geobacter sulfurreducens pili represent a novel class of electronically functional proteins.
- Experimental structural data are essential for accurate modeling and understanding protein conductivity.
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