ArticleNature communications2020
Cryo-EM structure of a Ca
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Chlorophyll reconstitution of photosynthetic light-harvesting complexes.Plant & cell physiology · 2025Review
- 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
- Probing the Dual Role of CaBiomolecules · 2025Article
- A Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.Communications biology · 2025Article
- Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum.Communications biology · 2024Article
- Tunneling Mechanisms of Quinones in Photosynthetic Reaction Center-Light Harvesting 1 Supercomplexes.Small science · 2024Article
- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 2024Article
- High-resolution structure and biochemical properties of the LH1-RC photocomplex from the model purple sulfur bacterium, Allochromatium vinosum.Communications biology · 2024Article
- Enhancing solar spectrum utilization in photosynthesis: exploring exciton and site energy shifts as key mechanisms.Scientific reports · 2023Article
- Article
- Atomic force microscopic analysis of the light-harvesting complex 2 from purple photosynthetic bacterium Thermochromatium tepidum.Photosynthesis research · 2023Article
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- Article
- Photosynthesis in the near infrared: the γ subunit of Blastochloris viridis LH1 red-shifts absorption beyond 1000 nm.The Biochemical journal · 2023Article
- Evaluation of the relationship between color-tuning of photosynthetic excitons and thermodynamic stability of light-harvesting chromoproteins.Photosynthetica · 2023Article
- Dominant role of excitons in photosynthetic color-tuning and light-harvesting.Frontiers in chemistry · 2023Article
- The role of the γ subunit in the photosystem of the lowest-energy phototrophs.The Biochemical journal · 2022Article
- An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.Communications biology · 2022Article
- Electronic Structure Effects Related to the Origin of the Remarkable Near-Infrared Absorption ofJournal of chemical theory and computation · 2022Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The light-harvesting-reaction center complex (LH1-RC) from the purple phototrophic bacterium Thiorhodovibrio strain 970 exhibits an LH1 absorption maximum at 960 nm, the most red-shifted absorption for any bacteriochlorophyll (BChl) a-containing species. Here we present a cryo-EM structure of the strain 970 LH1-RC complex at 2.82 Å resolution. The LH1 forms a closed ring structure composed of sixteen pairs of the αβ-polypeptides. Sixteen Ca ions are present in the LH1 C-terminal domain and are coordinated by residues from the αβ-polypeptides that are hydrogen-bonded to BChl a. The Ca
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.