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Thermally activated charge transport in microbial protein nanowires
The bacterium Geobacter sulfurreducens requires the expression of conductive protein filaments or pili to respire extracellular electron acceptors such as iron oxides and uranium and to wire electroactive biofilms, but the contribution of the protein fiber to charge transport has remained elusive. H...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4806346/ https://www.ncbi.nlm.nih.gov/pubmed/27009596 http://dx.doi.org/10.1038/srep23517 |
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author | Lampa-Pastirk, Sanela Veazey, Joshua P. Walsh, Kathleen A. Feliciano, Gustavo T. Steidl, Rebecca J. Tessmer, Stuart H. Reguera, Gemma |
author_facet | Lampa-Pastirk, Sanela Veazey, Joshua P. Walsh, Kathleen A. Feliciano, Gustavo T. Steidl, Rebecca J. Tessmer, Stuart H. Reguera, Gemma |
author_sort | Lampa-Pastirk, Sanela |
collection | PubMed |
description | The bacterium Geobacter sulfurreducens requires the expression of conductive protein filaments or pili to respire extracellular electron acceptors such as iron oxides and uranium and to wire electroactive biofilms, but the contribution of the protein fiber to charge transport has remained elusive. Here we demonstrate efficient long-range charge transport along individual pili purified free of metal and redox organic cofactors at rates high enough to satisfy the respiratory rates of the cell. Carrier characteristics were within the orders reported for organic semiconductors (mobility) and inorganic nanowires (concentration), and resistivity was within the lower ranges reported for moderately doped silicon nanowires. However, the pilus conductance and the carrier mobility decreased when one of the tyrosines of the predicted axial multistep hopping path was replaced with an alanine. Furthermore, low temperature scanning tunneling microscopy demonstrated the thermal dependence of the differential conductance at the low voltages that operate in biological systems. The results thus provide evidence for thermally activated multistep hopping as the mechanism that allows Geobacter pili to function as protein nanowires between the cell and extracellular electron acceptors. |
format | Online Article Text |
id | pubmed-4806346 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48063462016-03-25 Thermally activated charge transport in microbial protein nanowires Lampa-Pastirk, Sanela Veazey, Joshua P. Walsh, Kathleen A. Feliciano, Gustavo T. Steidl, Rebecca J. Tessmer, Stuart H. Reguera, Gemma Sci Rep Article The bacterium Geobacter sulfurreducens requires the expression of conductive protein filaments or pili to respire extracellular electron acceptors such as iron oxides and uranium and to wire electroactive biofilms, but the contribution of the protein fiber to charge transport has remained elusive. Here we demonstrate efficient long-range charge transport along individual pili purified free of metal and redox organic cofactors at rates high enough to satisfy the respiratory rates of the cell. Carrier characteristics were within the orders reported for organic semiconductors (mobility) and inorganic nanowires (concentration), and resistivity was within the lower ranges reported for moderately doped silicon nanowires. However, the pilus conductance and the carrier mobility decreased when one of the tyrosines of the predicted axial multistep hopping path was replaced with an alanine. Furthermore, low temperature scanning tunneling microscopy demonstrated the thermal dependence of the differential conductance at the low voltages that operate in biological systems. The results thus provide evidence for thermally activated multistep hopping as the mechanism that allows Geobacter pili to function as protein nanowires between the cell and extracellular electron acceptors. Nature Publishing Group 2016-03-24 /pmc/articles/PMC4806346/ /pubmed/27009596 http://dx.doi.org/10.1038/srep23517 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Lampa-Pastirk, Sanela Veazey, Joshua P. Walsh, Kathleen A. Feliciano, Gustavo T. Steidl, Rebecca J. Tessmer, Stuart H. Reguera, Gemma Thermally activated charge transport in microbial protein nanowires |
title | Thermally activated charge transport in microbial protein nanowires |
title_full | Thermally activated charge transport in microbial protein nanowires |
title_fullStr | Thermally activated charge transport in microbial protein nanowires |
title_full_unstemmed | Thermally activated charge transport in microbial protein nanowires |
title_short | Thermally activated charge transport in microbial protein nanowires |
title_sort | thermally activated charge transport in microbial protein nanowires |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4806346/ https://www.ncbi.nlm.nih.gov/pubmed/27009596 http://dx.doi.org/10.1038/srep23517 |
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