Cryo-EM and femtosecond spectroscopic studies provide mechanistic insight into the energy transfer in CpcL-phycobilisomes.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 37407580.
- Also identified by DOI 10.1038/s41467-023-39689-7 and PMC identifier 10322944.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Phycobilisomes
- Synechocystis