Evidence map›Paper›PMID 25416784›Full record

ArticleThe Journal of biological chemistry2015

Experimental evidence for a hydride transfer mechanism in plant glycolate oxidase catalysis.

Younès Dellero, Caroline Mauve, Edouard Boex-Fontvieille, Valérie Flesch, Mathieu Jossier, Guillaume Tcherkez, Michael Hodges

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. DspA/E-Triggered Non-Host Resistance againstInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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 2 institutions in 1 country.

Younès DelleroFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France.
Caroline MauveFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France, Plateforme Métabolisme-Métabolome, Saclay Plant Sciences, Institut de Biologie des Plantes, Bâtiment 630, 91405 Orsay Cedex, France, and.
Edouard Boex-FontvieilleFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France.
Valérie FleschFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France.
Mathieu JossierFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France.
Guillaume TcherkezFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France, Plateforme Métabolisme-Métabolome, Saclay Plant Sciences, Institut de Biologie des Plantes, Bâtiment 630, 91405 Orsay Cedex, France, and Institut Universitaire de France, 103 Boulevard Saint-Michel, 75005 Paris, France.
Michael HodgesFrom the Institut de Biologie des Plantes, CNRS UMR8618, Saclay Plant Sciences, Bâtiment 630, Université Paris Sud, 91405 Orsay Cedex, France, michael.hodges@u-psud.fr.
Université Paris-Sud · FRInstitut des Sciences des Plantes de Paris Saclay · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, glycolate oxidase is involved in the photorespiratory cycle, one of the major fluxes at the global scale. To clarify both the nature of the mechanism and possible differences in glycolate oxidase enzyme chemistry from C3 and C4 plant species, we analyzed kinetic parameters of purified recombinant C3 (Arabidopsis thaliana) and C4 (Zea mays) plant enzymes and compared isotope effects using natural and deuterated glycolate in either natural or deuterated solvent. The (12)C/(13)C isotope effect was also investigated for each plant glycolate oxidase protein by measuring the (13)C natural abundance in glycolate using natural or deuterated glycolate as a substrate. Our results suggest that several elemental steps were associated with an hydrogen/deuterium isotope effect and that glycolate α-deprotonation itself was only partially rate-limiting. Calculations of commitment factors from observed kinetic isotope effect values support a hydride transfer mechanism. No significant differences were seen between C3 and C4 enzymes.

Indexed as

Alcohol OxidoreductasesArabidopsisCarbon IsotopesCatalysisDeuteriumEscherichia coliLightModels, ChemicalPlant ExtractsPlant LeavesPlant Physiological PhenomenaPlant ProteinsProtein BindingProtein ConformationSolventsZea maysAlcohol OxidoreductasesCarbon IsotopesDeuteriumglycollate oxidasePlant ExtractsPlant ProteinsSolventsCatalysisEnzymeGlycolate OxidaseHydride TransferIsotope EffectOxidasePhotorespirationPlant

Identifiers

PMID25416784
PMCPMC4340412
OpenAlexW1965764801

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.