ArticleThe Journal of biological chemistry2022
Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls d and f.
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 33 papers.
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Who cites it
33 citing papers in PubMed, 80 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Red Light Enhances Biomass and Bioactive Compounds Through Photosynthetic Acclimation inMarine drugs · 2026Article
- The contribution of thePhotosynthesis research · 2026Article
- Mapping the absorption landscape of far-red Photosystem II.Nature communications · 2026Article
- Modified chlorophyll pigment at ChlChemical science · 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
- Chlorophyll Pigments and Their Synthetic Analogs.Plant & cell physiology · 2025Review
- Physical properties of chlorophyll-quinone conjugates prepared via Friedel-Crafts reaction.Photosynthesis research · 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
- Absorption changes in Photosystem II in the Soret band region upon the formation of the chlorophyll cation radical [PPhotosynthesis research · 2024Article
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Bicarbonate is a key regulator but not a substrate for OPhotosynthesis research · 2024Review
- Recent structural discoveries of photosystems I and II acclimated to absorb far-red light.Biochimica et biophysica acta. Bioenergetics · 2024Review
- Integrated Physiologic and Proteomic Analyses Reveal the Molecular Mechanism ofInternational journal of molecular sciences · 2024Article
- Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335.The Journal of biological chemistry · 2024Article
- Adaptation processes inFrontiers in plant science · 2024Review
- Common loss of far-red light photoacclimation in cyanobacteria from hot and cold deserts: a case study in the Chroococcidiopsidales.ISME communications · 2023Article
- Modeling the Characteristic Residues of ChlorophyllMicroorganisms · 2023Article
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Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Far-red light (FRL) photoacclimation in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700-800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light. These new Chls effectively lower the energy canonically thought to define the "red limit" for light required to drive photochemical catalysis of water oxidation. Changes to the architecture of FRL-PSII were previously unknown, and the positions of Chl d and Chl f molecules had only been proposed from indirect evidence. Here, we describe the 2.25 Å resolution cryo-EM structure of a monomeric FRL-PSII core complex from Synechococcus sp. PCC 7335 cells that were acclimated to FRL. We identify one Chl d molecule in the Chl
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