Uphill energy transfer mechanism for photosynthesis in an Antarctic alga.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 02 2023
15 02 2023
Historique:
received:
27
07
2021
accepted:
20
01
2023
entrez:
15
2
2023
pubmed:
16
2
2023
medline:
18
2
2023
Statut:
epublish
Résumé
Prasiola crispa, an aerial green alga, forms layered colonies under the severe terrestrial conditions of Antarctica. Since only far-red light is available at a deep layer of the colony, P. crispa has evolved a molecular system for photosystem II (PSII) excitation using far-red light with uphill energy transfer. However, the molecular basis underlying this system remains elusive. Here, we purified a light-harvesting chlorophyll (Chl)-binding protein complex from P. crispa (Pc-frLHC) that excites PSII with far-red light and revealed its ring-shaped structure with undecameric 11-fold symmetry at 3.13 Å resolution. The primary structure suggests that Pc-frLHC evolved from LHCI rather than LHCII. The circular arrangement of the Pc-frLHC subunits is unique among eukaryote LHCs and forms unprecedented Chl pentamers at every subunit‒subunit interface near the excitation energy exit sites. The Chl pentamers probably contribute to far-red light absorption. Pc-frLHC's unique Chl arrangement likely promotes PSII excitation with entropy-driven uphill excitation energy transfer.
Identifiants
pubmed: 36792917
doi: 10.1038/s41467-023-36245-1
pii: 10.1038/s41467-023-36245-1
pmc: PMC9931709
doi:
Substances chimiques
Photosystem I Protein Complex
0
Photosystem II Protein Complex
0
Light-Harvesting Protein Complexes
0
Chlorophyll
1406-65-1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
730Informations de copyright
© 2023. The Author(s).
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