Evidence map›Paper›PMID 28894198›Full record

ArticleScientific reports2017

Functional modulation of LHCSR1 protein from Physcomitrella patens by zeaxanthin binding and low pH.

Alberta Pinnola, Matteo Ballottari, Ilaria Bargigia, Marcelo Alcocer, Cosimo D'Andrea, Giulio Cerullo, Roberto Bassi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

  1. LHCSR1 Functions as a Dimmer Switch for Light Harvesting.The journal of physical chemistry letters · 2026
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  9. Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. LHCSR3 is a nonphotochemical quencher of both photosystems inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Combination of the EndogenousFrontiers in plant science · 2017
    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

7 authors at 3 institutions in 1 country.

Alberta PinnolaDipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, I-37134, Verona, Italy.
Matteo BallottariDipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, I-37134, Verona, Italy.
Ilaria BargigiaCenter for Nano Science and Technology @PoliMi, Istituto Italiano di Tecnologia, via Pascoli 70/3, 20133, Milano, Italy.
Marcelo AlcocerCenter for Nano Science and Technology @PoliMi, Istituto Italiano di Tecnologia, via Pascoli 70/3, 20133, Milano, Italy.ORCID 0000-0002-6600-1335
Cosimo D'AndreaCenter for Nano Science and Technology @PoliMi, Istituto Italiano di Tecnologia, via Pascoli 70/3, 20133, Milano, Italy.
Giulio CerulloIFN-CNR, Department of Physics, Politecnico di Milano, P.za L. da Vinci 32, 20133, Milano, Italy.
Roberto BassiDipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, I-37134, Verona, Italy. roberto.bassi@univr.it.ORCID 0000-0002-4140-8446
Italian Institute of Technology · ITUniversity of Verona · ITPolitecnico di Milano · IT

Funding

European Research Council 679814
6 · The paper itself

Abstract

Light harvesting for oxygenic photosynthesis is regulated to prevent the formation of harmful photoproducts by activation of photoprotective mechanisms safely dissipating the energy absorbed in excess. Lumen acidification is the trigger for the formation of quenching states in pigment binding complexes. With the aim to uncover the photoprotective functional states responsible for excess energy dissipation in green algae and mosses, we compared the fluorescence dynamic properties of the light-harvesting complex stress-related (LHCSR1) protein, which is essential for fast and reversible regulation of light use efficiency in lower plants, as compared to the major LHCII antenna protein, which mainly fulfills light harvesting function. Both LHCII and LHCSR1 had a chlorophyll fluorescence yield and lifetime strongly dependent on detergent concentration but the transition from long- to short-living states was far more complete and fast in the latter. Low pH and zeaxanthin binding enhanced the relative amplitude of quenched states in LHCSR1, which were characterized by the presence of 80 ps fluorescence decay components with a red-shifted emission spectrum. We suggest that energy dissipation occurs in the chloroplast by the activation of 80 ps quenching sites in LHCSR1 which spill over excitons from the photosystem II antenna system.

Indexed as

Hydrogen-Ion ConcentrationBryopsidaPigments, BiologicalPlant ProteinsProtein BindingRecombinant ProteinsSpectrum AnalysisZeaxanthinsPigments, BiologicalPlant ProteinsRecombinant ProteinsZeaxanthins

Identifiers

PMID28894198
PMCPMC5593824
OpenAlexW2751542984

What OpenQuestion holds

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LicenceCC BY
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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.