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Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c
Photosynthesis converts light energy to chemical energy to fuel life on earth. Light energy is harvested by antenna pigments and transferred to reaction centers (RCs) to drive the electron transfer (ET) reactions. Here, we present cryo-electron microscopy (cryo-EM) structures of two forms of the RC...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9751088/ https://www.ncbi.nlm.nih.gov/pubmed/36517472 http://dx.doi.org/10.1038/s41467-022-35460-6 |
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author | Dong, Shishang Huang, Guoqiang Wang, Changhui Wang, Jiajia Sui, Sen-Fang Qin, Xiaochun |
author_facet | Dong, Shishang Huang, Guoqiang Wang, Changhui Wang, Jiajia Sui, Sen-Fang Qin, Xiaochun |
author_sort | Dong, Shishang |
collection | PubMed |
description | Photosynthesis converts light energy to chemical energy to fuel life on earth. Light energy is harvested by antenna pigments and transferred to reaction centers (RCs) to drive the electron transfer (ET) reactions. Here, we present cryo-electron microscopy (cryo-EM) structures of two forms of the RC from the microaerophilic Chloracidobacterium thermophilum (CabRC): one containing 10 subunits, including two different cytochromes; and the other possessing two additional subunits, PscB and PscZ. The larger form contained 2 Zn-bacteriochlorophylls, 16 bacteriochlorophylls, 10 chlorophylls, 2 lycopenes, 2 hemes, 3 Fe(4)S(4) clusters, 12 lipids, 2 Ca(2+) ions and 6 water molecules, revealing a type I RC with an ET chain involving two hemes and a hybrid antenna containing bacteriochlorophylls and chlorophylls. Our results provide a structural basis for understanding the excitation energy and ET within the CabRC and offer evolutionary insights into the origin and adaptation of photosynthetic RCs. |
format | Online Article Text |
id | pubmed-9751088 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-97510882022-12-16 Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c Dong, Shishang Huang, Guoqiang Wang, Changhui Wang, Jiajia Sui, Sen-Fang Qin, Xiaochun Nat Commun Article Photosynthesis converts light energy to chemical energy to fuel life on earth. Light energy is harvested by antenna pigments and transferred to reaction centers (RCs) to drive the electron transfer (ET) reactions. Here, we present cryo-electron microscopy (cryo-EM) structures of two forms of the RC from the microaerophilic Chloracidobacterium thermophilum (CabRC): one containing 10 subunits, including two different cytochromes; and the other possessing two additional subunits, PscB and PscZ. The larger form contained 2 Zn-bacteriochlorophylls, 16 bacteriochlorophylls, 10 chlorophylls, 2 lycopenes, 2 hemes, 3 Fe(4)S(4) clusters, 12 lipids, 2 Ca(2+) ions and 6 water molecules, revealing a type I RC with an ET chain involving two hemes and a hybrid antenna containing bacteriochlorophylls and chlorophylls. Our results provide a structural basis for understanding the excitation energy and ET within the CabRC and offer evolutionary insights into the origin and adaptation of photosynthetic RCs. Nature Publishing Group UK 2022-12-14 /pmc/articles/PMC9751088/ /pubmed/36517472 http://dx.doi.org/10.1038/s41467-022-35460-6 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Dong, Shishang Huang, Guoqiang Wang, Changhui Wang, Jiajia Sui, Sen-Fang Qin, Xiaochun Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title_full | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title_fullStr | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title_full_unstemmed | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title_short | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c |
title_sort | structure of the acidobacteria homodimeric reaction center bound with cytochrome c |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9751088/ https://www.ncbi.nlm.nih.gov/pubmed/36517472 http://dx.doi.org/10.1038/s41467-022-35460-6 |
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