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An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation
The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-bindi...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6303296/ https://www.ncbi.nlm.nih.gov/pubmed/30575735 http://dx.doi.org/10.1038/s41467-018-07839-x |
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author | Duarte, Américo G. Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio M. Sousa, Filipa L. Clarke, Thomas A. Pereira, Inês A. C. |
author_facet | Duarte, Américo G. Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio M. Sousa, Filipa L. Clarke, Thomas A. Pereira, Inês A. C. |
author_sort | Duarte, Américo G. |
collection | PubMed |
description | The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-binding sites of the QrcABCD complex are periplasmic, and their role in energy conservation has not been elucidated. Here we show that the QrcABCD complex of Desulfovibrio vulgaris is electrogenic, as protons and electrons required for quinone reduction are extracted from opposite sides of the membrane, with a H(+)/e(−) ratio of 1. Although the complex does not act as a H(+)-pump, QrcD may include a conserved proton channel leading from the N-side to the P-side menaquinone pocket. Our work provides evidence of how energy is conserved during dissimilatory sulfate reduction, and suggests mechanisms behind the functions of related bacterial respiratory complexes in other bioenergetic contexts. |
format | Online Article Text |
id | pubmed-6303296 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63032962018-12-23 An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation Duarte, Américo G. Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio M. Sousa, Filipa L. Clarke, Thomas A. Pereira, Inês A. C. Nat Commun Article The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-binding sites of the QrcABCD complex are periplasmic, and their role in energy conservation has not been elucidated. Here we show that the QrcABCD complex of Desulfovibrio vulgaris is electrogenic, as protons and electrons required for quinone reduction are extracted from opposite sides of the membrane, with a H(+)/e(−) ratio of 1. Although the complex does not act as a H(+)-pump, QrcD may include a conserved proton channel leading from the N-side to the P-side menaquinone pocket. Our work provides evidence of how energy is conserved during dissimilatory sulfate reduction, and suggests mechanisms behind the functions of related bacterial respiratory complexes in other bioenergetic contexts. Nature Publishing Group UK 2018-12-21 /pmc/articles/PMC6303296/ /pubmed/30575735 http://dx.doi.org/10.1038/s41467-018-07839-x Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Duarte, Américo G. Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio M. Sousa, Filipa L. Clarke, Thomas A. Pereira, Inês A. C. An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title | An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title_full | An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title_fullStr | An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title_full_unstemmed | An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title_short | An electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
title_sort | electrogenic redox loop in sulfate reduction reveals a likely widespread mechanism of energy conservation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6303296/ https://www.ncbi.nlm.nih.gov/pubmed/30575735 http://dx.doi.org/10.1038/s41467-018-07839-x |
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