Evidence map›Paper›PMID 32005811›Full record

ArticleNature communications2020

Charge transfer from the carotenoid can quench chlorophyll excitation in antenna complexes of plants.

Lorenzo Cupellini, Dario Calvani, Denis Jacquemin, Benedetta Mennucci

Open access · goldAbstract read
In one paragraph

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
7.4field-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

37 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
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  8. Chlorophyll to zeaxanthin energy transfer in nonphotochemical quenching: An exciton annihilation-free transient absorption study.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Multi-Step and Switchable Energy Transfer in Photoluminescent Organosilicone Capsules.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The origin of pigment-binding differences in CP29 and LHCII: the role of protein structure and dynamics.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. Machine Learning Exciton Hamiltonians in Light-Harvesting Complexes.Journal of chemical theory and computation · 2023
    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 2 institutions in 2 countries.

Lorenzo CupelliniUniversità di Pisa, Dipartimento di Chimica e Chimica Industriale, Via G. Moruzzi 13, 56124, Pisa, (PI), Italy. lorenzo.cupellini@unipi.it.ORCID http://orcid.org/0000-0003-0848-2908
Dario CalvaniUniversità di Pisa, Dipartimento di Chimica e Chimica Industriale, Via G. Moruzzi 13, 56124, Pisa, (PI), Italy.ORCID http://orcid.org/0000-0002-3106-4061
Denis JacqueminLaboratoire CEISAM-UMR CNRS 6230, Université de Nantes, 2 Rue de la Houssiniere, BP-92208, F-44322 Cedex 3, Nantes, France.ORCID http://orcid.org/0000-0002-4217-0708
Benedetta MennucciUniversità di Pisa, Dipartimento di Chimica e Chimica Industriale, Via G. Moruzzi 13, 56124, Pisa, (PI), Italy. benedetta.mennucci@unipi.it.ORCID http://orcid.org/0000-0002-4394-0129
University of Pisa · ITCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The photosynthetic apparatus of higher plants can dissipate excess excitation energy during high light exposure, by deactivating excited chlorophylls through a mechanism called nonphotochemical quenching (NPQ). However, the precise molecular details of quenching and the mechanism regulating the quenching level are still not completely understood. Focusing on the major light-harvesting complex LHCII of Photosystem II, we show that a charge transfer state involving Lutein can efficiently quench chlorophyll excitation, and reduce the excitation lifetime of LHCII to the levels measured in the deeply quenched LHCII aggregates. Through a combination of molecular dynamics simulations, multiscale quantum chemical calculations, and kinetic modeling, we demonstrate that the quenching level can be finely tuned by the protein, by regulating the energy of the charge transfer state. Our results suggest that a limited conformational rearrangement of the protein scaffold could act as a molecular switch to activate or deactivate the quenching mechanism.

Indexed as

CarotenoidsChlorophyllElectron TransportKineticsLightLight-Harvesting Protein ComplexesPhotosynthesisPhotosystem II Protein ComplexPlantsCarotenoidsChlorophyllLight-Harvesting Protein ComplexesPhotosystem II Protein Complex

Identifiers

PMID32005811
PMCPMC6994720
OpenAlexW3003593958

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.