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Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes
Phycobilisomes (PBS) are the major light harvesting complexes of photosynthesis in the cyanobacteria and red algae. CpcL-PBS is a type of small PBS in cyanobacteria that transfers energy directly to photosystem I without the core structure. Here we report the cryo-EM structure of the CpcL-PBS from t...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10322944/ https://www.ncbi.nlm.nih.gov/pubmed/37407580 http://dx.doi.org/10.1038/s41467-023-39689-7 |
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author | Zheng, Lvqin Zhang, Zhengdong Wang, Hongrui Zheng, Zhenggao Wang, Jiayu Liu, Heyuan Chen, Hailong Dong, Chunxia Wang, Guopeng Weng, Yuxiang Gao, Ning Zhao, Jindong |
author_facet | Zheng, Lvqin Zhang, Zhengdong Wang, Hongrui Zheng, Zhenggao Wang, Jiayu Liu, Heyuan Chen, Hailong Dong, Chunxia Wang, Guopeng Weng, Yuxiang Gao, Ning Zhao, Jindong |
author_sort | Zheng, Lvqin |
collection | PubMed |
description | Phycobilisomes (PBS) are the major light harvesting complexes of photosynthesis in the cyanobacteria and red algae. CpcL-PBS is a type of small PBS in cyanobacteria that transfers energy directly to photosystem I without the core structure. Here we report the cryo-EM structure of the CpcL-PBS from the cyanobacterium Synechocystis sp. PCC 6803 at 2.6-Å resolution. The structure shows the CpcD domain of ferredoxin: NADP(+) oxidoreductase is located at the distal end of CpcL-PBS, responsible for its attachment to PBS. With the evidence of ultrafast transient absorption and fluorescence spectroscopy, the roles of individual bilins in energy transfer are revealed. The bilin (1I)β(82)(2) located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I. |
format | Online Article Text |
id | pubmed-10322944 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-103229442023-07-07 Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes Zheng, Lvqin Zhang, Zhengdong Wang, Hongrui Zheng, Zhenggao Wang, Jiayu Liu, Heyuan Chen, Hailong Dong, Chunxia Wang, Guopeng Weng, Yuxiang Gao, Ning Zhao, Jindong Nat Commun Article Phycobilisomes (PBS) are the major light harvesting complexes of photosynthesis in the cyanobacteria and red algae. CpcL-PBS is a type of small PBS in cyanobacteria that transfers energy directly to photosystem I without the core structure. Here we report the cryo-EM structure of the CpcL-PBS from the cyanobacterium Synechocystis sp. PCC 6803 at 2.6-Å resolution. The structure shows the CpcD domain of ferredoxin: NADP(+) oxidoreductase is located at the distal end of CpcL-PBS, responsible for its attachment to PBS. With the evidence of ultrafast transient absorption and fluorescence spectroscopy, the roles of individual bilins in energy transfer are revealed. The bilin (1I)β(82)(2) located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I. Nature Publishing Group UK 2023-07-05 /pmc/articles/PMC10322944/ /pubmed/37407580 http://dx.doi.org/10.1038/s41467-023-39689-7 Text en © The Author(s) 2023 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Zheng, Lvqin Zhang, Zhengdong Wang, Hongrui Zheng, Zhenggao Wang, Jiayu Liu, Heyuan Chen, Hailong Dong, Chunxia Wang, Guopeng Weng, Yuxiang Gao, Ning Zhao, Jindong Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title_full | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title_fullStr | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title_full_unstemmed | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title_short | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes |
title_sort | cryo-em and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in cpcl-phycobilisomes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10322944/ https://www.ncbi.nlm.nih.gov/pubmed/37407580 http://dx.doi.org/10.1038/s41467-023-39689-7 |
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