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Evolution of complex I–like respiratory complexes
The modern-day respiratory complex I shares a common ancestor with the membrane-bound hydrogenase (MBH) and membrane-bound sulfane sulfur reductase (MBS). MBH and MBS use protons and sulfur as their respective electron sinks, which helped to conserve energy during early life in the Proterozoic era w...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8165549/ https://www.ncbi.nlm.nih.gov/pubmed/33957129 http://dx.doi.org/10.1016/j.jbc.2021.100740 |
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author | Yu, Hongjun Schut, Gerrit J. Haja, Domink K. Adams, Michael W.W. Li, Huilin |
author_facet | Yu, Hongjun Schut, Gerrit J. Haja, Domink K. Adams, Michael W.W. Li, Huilin |
author_sort | Yu, Hongjun |
collection | PubMed |
description | The modern-day respiratory complex I shares a common ancestor with the membrane-bound hydrogenase (MBH) and membrane-bound sulfane sulfur reductase (MBS). MBH and MBS use protons and sulfur as their respective electron sinks, which helped to conserve energy during early life in the Proterozoic era when the Earth's atmosphere was low in oxygen. MBH and MBS likely evolved from an integration of an ancestral, membrane-embedded, multiple resistance and pH antiporter and a soluble redox-active module encompassing a [NiFe] hydrogenase. In this review, we discuss how the structures of MBH, MBS, multiple resistance and pH, photosynthetic NADH dehydrogenase-like complex type-1, and complex I, which have been determined recently, thanks to the advent of high-resolution cryo-EM, have significantly improved our understanding of the catalytic reaction mechanisms and the evolutionary relationships of the respiratory complexes. |
format | Online Article Text |
id | pubmed-8165549 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-81655492021-06-05 Evolution of complex I–like respiratory complexes Yu, Hongjun Schut, Gerrit J. Haja, Domink K. Adams, Michael W.W. Li, Huilin J Biol Chem JBC Reviews The modern-day respiratory complex I shares a common ancestor with the membrane-bound hydrogenase (MBH) and membrane-bound sulfane sulfur reductase (MBS). MBH and MBS use protons and sulfur as their respective electron sinks, which helped to conserve energy during early life in the Proterozoic era when the Earth's atmosphere was low in oxygen. MBH and MBS likely evolved from an integration of an ancestral, membrane-embedded, multiple resistance and pH antiporter and a soluble redox-active module encompassing a [NiFe] hydrogenase. In this review, we discuss how the structures of MBH, MBS, multiple resistance and pH, photosynthetic NADH dehydrogenase-like complex type-1, and complex I, which have been determined recently, thanks to the advent of high-resolution cryo-EM, have significantly improved our understanding of the catalytic reaction mechanisms and the evolutionary relationships of the respiratory complexes. American Society for Biochemistry and Molecular Biology 2021-05-03 /pmc/articles/PMC8165549/ /pubmed/33957129 http://dx.doi.org/10.1016/j.jbc.2021.100740 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | JBC Reviews Yu, Hongjun Schut, Gerrit J. Haja, Domink K. Adams, Michael W.W. Li, Huilin Evolution of complex I–like respiratory complexes |
title | Evolution of complex I–like respiratory complexes |
title_full | Evolution of complex I–like respiratory complexes |
title_fullStr | Evolution of complex I–like respiratory complexes |
title_full_unstemmed | Evolution of complex I–like respiratory complexes |
title_short | Evolution of complex I–like respiratory complexes |
title_sort | evolution of complex i–like respiratory complexes |
topic | JBC Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8165549/ https://www.ncbi.nlm.nih.gov/pubmed/33957129 http://dx.doi.org/10.1016/j.jbc.2021.100740 |
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