ArticleThe Biochemical journal2021
Cryo-EM structure of the dimeric Rhodobacter sphaeroides RC-LH1 core complex at 2.9 Å: the structural basis for dimerisation.
Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- Molecular dissection of the Cereibacter sphaeroides spheroidene monooxygenase.The Biochemical journal · 2026Article
- Singlet fission mediates carotenoid-to-bacteriochlorophyll energy transfer in purple photosynthetic bacteria.Nature chemistry · 2026Article
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- Article
- Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A distinct double-ring LH1-LH2 photocomplex from an extremophilic phototroph.Nature communications · 2025Article
- Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum.Communications biology · 2024Article
- Architectures of photosynthetic RC-LH1 supercomplexes fromScience advances · 2024Article
- Tuning by Hydrogen Bonding in Photosynthesis.The journal of physical chemistry. B · 2024Article
- Single-Molecule Detection of the Encounter and Productive Electron Transfer Complexes of a Photosynthetic Reaction Center.Journal of the American Chemical Society · 2024Article
- Sulfoquinovosyl diacylglycerol is required for dimerisation of the Rhodobacter sphaeroides reaction centre-light harvesting 1 core complex.The Biochemical journal · 2024Article
- Excitation energy transfer in proteoliposomes reconstituted with LH2 and RC-LH1 complexes from Rhodobacter sphaeroides.Bioscience reports · 2024Article
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- Photosynthesis in the near infrared: the γ subunit of Blastochloris viridis LH1 red-shifts absorption beyond 1000 nm.The Biochemical journal · 2023Article
- Cryo-EM structure of the four-subunitProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.Nature communications · 2023Article
- Dominant role of excitons in photosynthetic color-tuning and light-harvesting.Frontiers in chemistry · 2023Article
- An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.Communications biology · 2022Article
- Algal photosystem I dimer and high-resolution model of PSI-plastocyanin complex.Nature plants · 2022Article
- Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.Nature communications · 2022Article
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Authors and funding
9 authors at 3 institutions in 5 countries.
Funding
Abstract
The dimeric reaction centre light-harvesting 1 (RC-LH1) core complex of Rhodobacter sphaeroides converts absorbed light energy to a charge separation, and then it reduces a quinone electron and proton acceptor to a quinol. The angle between the two monomers imposes a bent configuration on the dimer complex, which exerts a major influence on the curvature of the membrane vesicles, known as chromatophores, where the light-driven photosynthetic reactions take place. To investigate the dimerisation interface between two RC-LH1 monomers, we determined the cryogenic electron microscopy structure of the dimeric complex at 2.9 Å resolution. The structure shows that each monomer consists of a central RC partly enclosed by a 14-subunit LH1 ring held in an open state by PufX and protein-Y polypeptides, thus enabling quinones to enter and leave the complex. Two monomers are brought together through N-terminal interactions between PufX polypeptides on the cytoplasmic side of the complex, augmented by two novel transmembrane polypeptides, designated protein-Z, that bind to the outer faces of the two central LH1 β polypeptides. The precise fit at the dimer interface, enabled by PufX and protein-Z, by C-terminal interactions between opposing LH1 αβ subunits, and by a series of interactions with a bound sulfoquinovosyl diacylglycerol lipid, bring together each monomer creating an S-shaped array of 28 bacteriochlorophylls. The seamless join between the two sets of LH1 bacteriochlorophylls provides a path for excitation energy absorbed by one half of the complex to migrate across the dimer interface to the other half.
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