ArticleNature communications2023
Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 21 citations in OpenAlex.
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- Enhanced Production of Astaxanthin and Zeaxanthin by Paracoccus Sp. LL1 Through Random Mutagenesis.Biotechnology and applied biochemistry · 2026Article
- Chlorophyll reconstitution of photosynthetic light-harvesting complexes.Plant & cell physiology · 2025Review
- Significant Effects of Excitonic Coupling and Charge Transfer on the Circular Dichroism Spectrum of Photosynthetic Light-Harvesting I Complex.The journal of physical chemistry. B · 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
- Tunneling Mechanisms of Quinones in Photosynthetic Reaction Center-Light Harvesting 1 Supercomplexes.Small science · 2024Article
- Architectures of photosynthetic RC-LH1 supercomplexes fromScience advances · 2024Article
- Role of hydrogen-bond networks on the donor side of photosynthetic reaction centers from purple bacteria.Biophysical reviews · 2023Review
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- Characterization of the Structure and Function of the Photosynthetic RC-LH1 Core Supercomplex From Rhodospirillum rubrum.Physiologia plantarumArticle
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1-reaction center (LH1-RC) complex, but lacks protein-U, a U-shaped polypeptide in the LH1-RC of its close relative Rba. sphaeroides. Here we present a cryo-EM structure of the Rba. capsulatus LH1-RC purified by DEAE chromatography. The crescent-shaped LH1-RC exhibits a compact structure containing only 10 LH1 αβ-subunits. Four αβ-subunits corresponding to those adjacent to protein-U in Rba. sphaeroides were absent. PufX in Rba. capsulatus exhibits a unique conformation in its N-terminus that self-associates with amino acids in its own transmembrane domain and interacts with nearby polypeptides, preventing it from interacting with proteins in other complexes and forming dimeric structures. These features are discussed in relation to the minimal requirements for the formation of LH1-RC monomers and dimers, the spectroscopic behavior of both the LH1 and RC, and the bioenergetics of energy transfer from LH1 to the RC.
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