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

bacteriochlorophyll carotenoids cryogenic electron microscopy light-harvesting complex photosynthesis purple bacteria

Journal

Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797

Informations de publication

Date de publication:
31 05 2023
Historique:
received: 23 01 2023
revised: 12 04 2023
accepted: 25 04 2023
medline: 29 5 2023
pubmed: 26 4 2023
entrez: 26 4 2023
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 37098760
pii: 232981
doi: 10.1042/BSR20220089
pmc: PMC10214105
pii:
doi:

Substances chimiques

Carotenoids 36-88-4
quinone 3T006GV98U
Benzoquinones 0
Bacterial Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2023 The Author(s).

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Auteurs

David J K Swainsbury (DJK)

School of Biosciences, University of Sheffield, Sheffield, UK.
School of Biological Sciences, University of East Anglia, Norwich, UK.

Pu Qian (P)

Materials and Structural Analysis, Thermo Fisher Scientific, Eindhoven, Netherlands.

Andrew Hitchcock (A)

School of Biosciences, University of Sheffield, Sheffield, UK.

C Neil Hunter (CN)

School of Biosciences, University of Sheffield, Sheffield, UK.

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Classifications MeSH