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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...

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Autores principales: Dong, Shishang, Huang, Guoqiang, Wang, Changhui, Wang, Jiajia, Sui, Sen-Fang, Qin, Xiaochun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
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.
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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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