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Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target
Cytochrome bd is a triheme copper-free terminal oxidase in membrane respiratory chains of prokaryotes. This unique molecular machine couples electron transfer from quinol to O(2) with the generation of a proton motive force without proton pumping. Apart from energy conservation, the bd enzyme plays...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8951039/ https://www.ncbi.nlm.nih.gov/pubmed/35328590 http://dx.doi.org/10.3390/ijms23063166 |
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author | Friedrich, Thorsten Wohlwend, Daniel Borisov, Vitaliy B. |
author_facet | Friedrich, Thorsten Wohlwend, Daniel Borisov, Vitaliy B. |
author_sort | Friedrich, Thorsten |
collection | PubMed |
description | Cytochrome bd is a triheme copper-free terminal oxidase in membrane respiratory chains of prokaryotes. This unique molecular machine couples electron transfer from quinol to O(2) with the generation of a proton motive force without proton pumping. Apart from energy conservation, the bd enzyme plays an additional key role in the microbial cell, being involved in the response to different environmental stressors. Cytochrome bd promotes virulence in a number of pathogenic species that makes it a suitable molecular drug target candidate. This review focuses on recent advances in understanding the structure of cytochrome bd and the development of its selective inhibitors. |
format | Online Article Text |
id | pubmed-8951039 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89510392022-03-26 Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target Friedrich, Thorsten Wohlwend, Daniel Borisov, Vitaliy B. Int J Mol Sci Review Cytochrome bd is a triheme copper-free terminal oxidase in membrane respiratory chains of prokaryotes. This unique molecular machine couples electron transfer from quinol to O(2) with the generation of a proton motive force without proton pumping. Apart from energy conservation, the bd enzyme plays an additional key role in the microbial cell, being involved in the response to different environmental stressors. Cytochrome bd promotes virulence in a number of pathogenic species that makes it a suitable molecular drug target candidate. This review focuses on recent advances in understanding the structure of cytochrome bd and the development of its selective inhibitors. MDPI 2022-03-15 /pmc/articles/PMC8951039/ /pubmed/35328590 http://dx.doi.org/10.3390/ijms23063166 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Friedrich, Thorsten Wohlwend, Daniel Borisov, Vitaliy B. Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title | Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title_full | Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title_fullStr | Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title_full_unstemmed | Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title_short | Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target |
title_sort | recent advances in structural studies of cytochrome bd and its potential application as a drug target |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8951039/ https://www.ncbi.nlm.nih.gov/pubmed/35328590 http://dx.doi.org/10.3390/ijms23063166 |
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