Evidence map›Paper›PMID 37098760›Full record

ArticleBioscience reports2023

The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.

David J K Swainsbury, Pu Qian, Andrew Hitchcock, C Neil Hunter

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
7.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Trade-offs between light absorption and energy transfer in a marine light-harvesting complex 2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. CaThe journal of physical chemistry letters · 2026
    Article
  4. Article
  5. Photocatalytic Biohybrid Vesicles.Chemical reviews · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Mining thermophile photosynthesis genes: a synthetic operon expressingbioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Probing the Dual Role of CaBiomolecules · 2025
    Article
  14. Article
  15. Article
  16. Tuning by Hydrogen Bonding in Photosynthesis.The journal of physical chemistry. B · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

David J K SwainsburySchool of Biosciences, University of Sheffield, Sheffield, UK.ORCID 0000-0002-0754-0363
Pu QianMaterials and Structural Analysis, Thermo Fisher Scientific, Eindhoven, Netherlands.ORCID 0000-0002-5888-8546
Andrew HitchcockSchool of Biosciences, University of Sheffield, Sheffield, UK.ORCID 0000-0001-6572-434X
C Neil HunterSchool of Biosciences, University of Sheffield, Sheffield, UK.ORCID 0000-0003-2533-9783
University of Sheffield · GBThermo Fisher Scientific (Netherlands) · NLUniversity of East Anglia · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chlorophototrophic organisms have a charge-separating reaction centre (RC) complex that receives energy from a dedicated light-harvesting (LH) antenna. In the purple phototrophic bacteria, these two functions are embodied by the 'core' photosynthetic component, the RC-LH1 complex. RC-LH1 complexes sit within a membrane bilayer, with the central RC wholly or partly surrounded by a curved array of LH1 subunits that bind a series of bacteriochlorophyll (BChl) and carotenoid pigments. Decades of research have shown that the absorption of light initiates a cascade of energy, electron, and proton transfers that culminate in the formation of a quinol, which is subsequently oxidized by the cytochrome bc1 complex. However, a full understanding of all these processes, from femtosecond absorption of light to millisecond quinone diffusion, requires a level of molecular detail that was lacking until the remarkable recent upsurge in the availability of RC-LH1 structures. Here, we survey 13 recently determined RC-LH1 assemblies, and we compare the precise molecular arrangements of pigments and proteins that allow efficient light absorption and the transfer of energy, electrons and protons. We highlight shared structural features, as well as differences that span the bound pigments and cofactors, the structures of individual subunits, the overall architecture of the complexes, and the roles of additional subunits newly identified in just one or a few species. We discuss RC-LH1 structures in the context of prior biochemical and spectroscopic investigations, which together enhance our understanding of the molecular mechanisms of photosynthesis in the purple phototrophic bacteria. A particular emphasis is placed on how the remarkable and unexpected structural diversity in RC-LH1 complexes demonstrates different evolutionary solutions for maximising pigment density for optimised light harvesting, whilst balancing the requirement for efficient quinone diffusion between RC and cytochrome bc1 complexes through the encircling LH1 complex.

Indexed as

CarotenoidsPhotosynthesisBacteriaBacterial ProteinsBenzoquinonesCytoplasmBacterial ProteinsBenzoquinonesCarotenoidsquinonebacteriochlorophyllcarotenoidscryogenic electron microscopylight-harvesting complexphotosynthesispurple bacteria

Identifiers

PMID37098760
PMCPMC10214105
OpenAlexW4367047861

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.