Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes

Lvqin Zheng, Zhengdong Zhang, Hongrui Wang, Zhenggao Zheng, Jiayu Wang, Heyuan Liu, Hailong Chen, Chunxia Dong, Guopeng Wang, Yuxiang Weng (), Ning Gao () and Jindong Zhao ()
Additional contact information
Lvqin Zheng: Peking University
Zhengdong Zhang: Peking University
Hongrui Wang: Peking University
Zhenggao Zheng: Peking University
Jiayu Wang: Chinese Academy of Sciences
Heyuan Liu: Chinese Academy of Sciences
Hailong Chen: Chinese Academy of Sciences
Chunxia Dong: Peking University
Guopeng Wang: Peking University
Yuxiang Weng: Chinese Academy of Sciences
Ning Gao: Peking University
Jindong Zhao: Peking University

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract 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 1Iβ822 located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I.

Date: 2023
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DOI: 10.1038/s41467-023-39689-7

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