Evidence map›Paper›PMID 39058977›Full record

ArticleJournal of the American Chemical Society2024

The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.

Nicoletta Liguori, Ivo H M van Stokkum, Fernando Muzzopappa, John T M Kennis, Diana Kirilovsky, Roberta Croce

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Atomistic simulations reveal the photoactivation mechanism of a carotenoid-binding photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
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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

6 authors.

Nicoletta LiguoriDepartment of Physics and Astronomy and Institute for Lasers, Life and Biophotonics, Faculty of Science, Vrije Universiteit Amsterdam, de Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.ORCID 0000-0001-5695-4012
Ivo H M van StokkumDepartment of Physics and Astronomy and Institute for Lasers, Life and Biophotonics, Faculty of Science, Vrije Universiteit Amsterdam, de Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.ORCID 0000-0002-6143-2021
Fernando MuzzopappaInstitute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Université Paris-Sud, Université Paris-Saclay, 91198 Gif sur Yvette ,France.
John T M KennisDepartment of Physics and Astronomy and Institute for Lasers, Life and Biophotonics, Faculty of Science, Vrije Universiteit Amsterdam, de Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.ORCID 0000-0002-3563-2353
Diana KirilovskyInstitute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Université Paris-Sud, Université Paris-Saclay, 91198 Gif sur Yvette ,France.
Roberta CroceDepartment of Physics and Astronomy and Institute for Lasers, Life and Biophotonics, Faculty of Science, Vrije Universiteit Amsterdam, de Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyanobacteria were the first microorganisms that released oxygen into the atmosphere billions of years ago. To do it safely under intense sunlight, they developed strategies that prevent photooxidation in the photosynthetic membrane, by regulating the light-harvesting activity of their antenna complexes-the phycobilisomes-via the orange-carotenoid protein (OCP). This water-soluble protein interacts with the phycobilisomes and triggers nonphotochemical quenching (NPQ), a mechanism that safely dissipates overexcitation in the membrane. To date, the mechanism of action of OCP in performing NPQ is unknown. In this work, we performed ultrafast spectroscopy on a minimal NPQ system composed of the active domain of OCP bound to the phycobilisome core. The use of this system allowed us to disentangle the signal of the carotenoid from that of the bilins. Our results demonstrate that the binding to the phycobilisomes modifies the structure of the ketocarotenoid associated with OCP. We show that this molecular switch activates NPQ, by enabling excitation-energy transfer from the antenna pigments to the ketocarotenoid.

Indexed as

Bacterial ProteinsCarotenoidsCyanobacteriaPhycobilisomesBile PigmentsPhotochemical ProcessesBacterial ProteinsBile PigmentsCarotenoidsorange carotenoid protein, SynechocystisPhycobilisomes

Identifiers

PMID39058977
PMCPMC11311238

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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.