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Title | Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 3961, Year 2023 |
Publish date | Jul 5, 2023 |
Authors | Lvqin Zheng / Zhengdong Zhang / Hongrui Wang / Zhenggao Zheng / Jiayu Wang / Heyuan Liu / Hailong Chen / Chunxia Dong / Guopeng Wang / Yuxiang Weng / Ning Gao / Jindong Zhao / |
PubMed 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 ...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 β located near photosystem I has an enhanced planarity and is the red-bilin responsible for the direct energy transfer to photosystem I. |
External links | Nat Commun / PubMed:37407580 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.64 Å |
Structure data | EMDB-34724, PDB-8hfq: |
Chemicals | ChemComp-CYC: |
Source |
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Keywords | PHOTOSYNTHESIS / CpcL-phycobilisome / energy transfer / ferredoxin:NADP+ oxidoreductase / ultrafast spectroscopy |