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

Lvqin ZhengZhengdong ZhangHongrui WangZhenggao ZhengJiayu WangHeyuan LiuHailong ChenChunxia DongGuopeng WangYu-Xiang WengNing GaoJindong Zhao
Published in: Nature communications (2023)
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.
Keyphrases
  • energy transfer
  • quantum dots
  • single molecule
  • minimally invasive