ArticleThe Journal of biological chemistry2022
Structure of a photosystem I-ferredoxin complex from a marine cyanobacterium provides insights into far-red light photoacclimation.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 51 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Molecular design principles for Photosystem I-based biohybrid solar fuel catalysts.bioRxiv : the preprint server for biology · 2026Article
- Far-red light-driven photoautotrophy of chlorophyll f-producing cyanobacterium without red-shifted phycobilisome core complex.Photosynthesis research · 2025Article
- Physical properties of chlorophyll-quinone conjugates prepared via Friedel-Crafts reaction.Photosynthesis research · 2025Article
- Development of a TSR-based method for understanding structural relationships of cofactors and local environments in photosystem I.BMC bioinformatics · 2025Article
- Two new non-chlorophyllFrontiers in microbiology · 2025Article
- A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center.Photosynthesis research · 2024Article
- EPR studies of ferredoxin in spinach and cyanobacterial thylakoids related to photosystem I-driven NADPPhotosynthesis research · 2024Article
- Structure of a biohybrid photosystem I-platinum nanoparticle solar fuel catalyst.Nature communications · 2024Article
- Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871.Photosynthesis research · 2024Article
- Recent structural discoveries of photosystems I and II acclimated to absorb far-red light.Biochimica et biophysica acta. Bioenergetics · 2024Review
- Shining light on dinoflagellate photosystem I.Nature communications · 2024Article
- Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.The Journal of biological chemistry · 2024Article
- Article
- Microbial applications for sustainable space exploration beyond low Earth orbit.NPJ microgravity · 2023Review
- Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light.The Journal of biological chemistry · 2023Article
- Molecular diversity and evolution of far-red light-acclimated photosystem I.Frontiers in plant science · 2023Article
- Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 Å resolution.Communications biology · 2022Article
- Molecular Evolution of Far-Red Light-Acclimated Photosystem II.Microorganisms · 2022Article
- Adaptation of Cyanobacteria to the Endolithic Light Spectrum in Hyper-Arid Deserts.Microorganisms · 2022Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Far-red light photoacclimation exhibited by some cyanobacteria allows these organisms to use the far-red region of the solar spectrum (700-800 nm) for photosynthesis. Part of this process includes the replacement of six photosystem I (PSI) subunits with isoforms that confer the binding of chlorophyll (Chl) f molecules that absorb far-red light (FRL). However, the exact sites at which Chl f molecules are bound are still challenging to determine. To aid in the identification of Chl f-binding sites, we solved the cryo-EM structure of PSI from far-red light-acclimated cells of the cyanobacterium Synechococcus sp. PCC 7335. We identified six sites that bind Chl f with high specificity and three additional sites that are likely to bind Chl f at lower specificity. All of these binding sites are in the core-antenna regions of PSI, and Chl f was not observed among the electron transfer cofactors. This structural analysis also reveals both conserved and nonconserved Chl f-binding sites, the latter of which exemplify the diversity in FRL-PSI among species. We found that the FRL-PSI structure also contains a bound soluble ferredoxin, PetF1, at low occupancy, which suggests that ferredoxin binds less transiently than expected according to the canonical view of ferredoxin-binding to facilitate electron transfer. We suggest that this may result from structural changes in FRL-PSI that occur specifically during FRL photoacclimation.
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