ArticleThe Journal of biological chemistry2023
Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light.
Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Mapping the absorption landscape of far-red Photosystem II.Nature communications · 2026Article
- Tuning the F695 fluorescent state in photosystem II using site-directed mutagenesis in Synechocystis sp. PCC 6803.Photosynthesis research · 2026Article
- The Recombination Triplet State in the Far-Red Light Adapted Photosystem II Is Located at the ChlThe journal of physical chemistry letters · 2025Article
- Previously unrecognized diversity of far-red light-using terrestrial green algae and cyanobacteria.iScience · 2025Article
- Structure of a stripped-down and tuned-up far-red phycobilisome.Communications biology · 2025Article
- Microscopic basis of reaction center modulation in PsbA variants of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Far-red light-driven photoautotrophy of chlorophyll f-producing cyanobacterium without red-shifted phycobilisome core complex.Photosynthesis research · 2025Article
- A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center.Photosynthesis research · 2024Article
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Perspectives on improving photosynthesis to increase crop yield.The Plant cell · 2024Review
- Adaptive Evolution Signatures inMicroorganisms · 2024Article
- Recent structural discoveries of photosystems I and II acclimated to absorb far-red light.Biochimica et biophysica acta. Bioenergetics · 2024Review
- Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyllScience advances · 2024Article
- Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.The Journal of biological chemistry · 2024Article
- Modeling the Characteristic Residues of ChlorophyllMicroorganisms · 2023Article
- Molecular diversity and evolution of far-red light-acclimated photosystem I.Frontiers in plant science · 2023Article
- Enhancing the production of chlorophyll f in the cyanobacterium Synechocystis sp. PCC 6803.Physiologia plantarumArticle
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Photosystem II (PSII) is the water-splitting enzyme central to oxygenic photosynthesis. To drive water oxidation, light is harvested by accessory pigments, mostly chlorophyll (Chl) a molecules, which absorb visible light (400-700 nm). Some cyanobacteria facultatively acclimate to shaded environments by altering their photosynthetic machinery to additionally absorb far-red light (FRL, 700-800 nm), a process termed far-red light photoacclimation or FaRLiP. During far-red light photoacclimation, FRL-PSII is assembled with FRL-specific isoforms of the subunits PsbA, PsbB, PsbC, PsbD, and PsbH, and some Chl-binding sites contain Chls d or f instead of the usual Chl a. The structure of an apo-FRL-PSII monomer lacking the FRL-specific PsbH subunit has previously been determined, but visualization of the dimeric complex has remained elusive. Here, we report the cryo-EM structure of a dimeric FRL-PSII complex. The site assignments for Chls d and f are consistent with those assigned in the previous apo-FRL-PSII monomeric structure. All sites that bind Chl d or Chl f at high occupancy exhibit a FRL-specific interaction of the formyl moiety of the Chl d or Chl f with the protein environment, which in some cases involves a phenylalanine sidechain. The structure retains the FRL-specific PsbH2 subunit, which appears to alter the energetic landscape of FRL-PSII, redirecting energy transfer from the phycobiliprotein complex to a Chl f molecule bound by PsbB2 that acts as a bridge for energy transfer to the electron transfer chain. Collectively, these observations extend our previous understanding of the structure-function relationship that allows PSII to function using lower energy FRL.
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