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 et al. · Nat Commun · 2023

basic_science · Level V

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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<sup>+</sup> 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 <sup>1I</sup>β<sup>82</sup><sub>2</sub> located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I.

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