Evidence map›Paper›PMID 19638474›Full record

ArticleThe Plant cell2009

A structural basis for the pH-dependent xanthophyll cycle in Arabidopsis thaliana.

Pascal Arnoux, Tomas Morosinotto, Giorgia Saga, Roberto Bassi, David Pignol

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

70 citing papers in PubMed, 170 citations in OpenAlex.

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  13. Modulation of xanthophyll cycle impacts biomass productivity in the marine microalgaProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  15. The Functions of Chloroplastic Ascorbate in Vascular Plants and Algae.International journal of molecular sciences · 2023
    Review
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  20. Review

10 more citing papers are in PubMed but not listed here.

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

5 authors at 4 institutions in 2 countries.

Pascal ArnouxCommissariat à l'Energie Atomique, Direction des Sciences du Vivant, Institut de Biologie Environementale et de Biotechnologie, Laboratoire de Bioénergétique Cellulaire, Saint-Paul-lez-Durance, F-13108, France.
Tomas Morosinotto
Giorgia Saga
Roberto Bassi
David Pignol
University of Padua · ITAix-Marseille Université · FRInstitute of Environmental Biology and Biotechnology · FRUniversity of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants adjust their photosynthetic activity to changing light conditions. A central regulation of photosynthesis depends on the xanthophyll cycle, in which the carotenoid violaxanthin is converted into zeaxanthin in strong light, thus activating the dissipation of the excess absorbed energy as heat and the scavenging of reactive oxygen species. Violaxanthin deepoxidase (VDE), the enzyme responsible for zeaxanthin synthesis, is activated by the acidification of the thylakoid lumen when photosynthetic electron transport exceeds the capacity of assimilatory reactions: at neutral pH, VDE is a soluble and inactive enzyme, whereas at acidic pH, it attaches to the thylakoid membrane where it binds its violaxanthin substrate. VDE also uses ascorbate as a cosubstrate with a pH-dependent Km that may reflect a preference for ascorbic acid. We determined the structures of the central lipocalin domain of VDE (VDEcd) at acidic and neutral pH. At neutral pH, VDEcd is monomeric with its active site occluded within a lipocalin barrel. Upon acidification, the barrel opens up and the enzyme appears as a dimer. A channel linking the two active sites of the dimer can harbor the entire carotenoid substrate and thus may permit the parallel deepoxidation of the two violaxanthin beta-ionone rings, making VDE an elegant example of the adaptation of an asymmetric enzyme to its symmetric substrate.

Indexed as

Amino Acid SequenceArabidopsisAscorbic AcidCrystallography, X-RayGene Expression Regulation, PlantHydrogen-Ion ConcentrationModels, MolecularMolecular Sequence DataOxidoreductasesPhotosynthesisProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidSubstrate SpecificityThylakoidsAscorbic AcidOxidoreductasesviolaxanthinviolaxanthin de-epoxidaseXanthophyllsZeaxanthins

Identifiers

PMID19638474
PMCPMC2729612
OpenAlexW2128675632

What OpenQuestion holds

Textmetadata
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.