Evidence map›Paper›PMID 22558308›Full record

ArticlePloS one2012

Crystal structure of ChrR--a quinone reductase with the capacity to reduce chromate.

Subramaniam Eswaramoorthy, Sébastien Poulain, Rainer Hienerwadel, Nicolas Bremond, Matthew D Sylvester, Yian-Biao Zhang, Catherine Berthomieu, Daniel Van Der Lelie, A Matin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. A Potent Quinone Reductase Encoded byMolecules (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Phenotypic and resistome analysis of antibiotic and heavy metal resistance in the Antarctic bacterium Pseudomonas sp. AU10.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. NfoR: Chromate Reductase or Flavin Mononucleotide Reductase?Applied and environmental microbiology · 2020
    Article
  13. Article
  14. Chromium Pollution in European Water, Sources, Health Risk, and Remediation Strategies: An Overview.International journal of environmental research and public health · 2020
    Review
  15. Article
  16. Extracellular Vesicle-MediatedMolecular cancer therapeutics · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. 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

9 authors at 5 institutions in 2 countries.

Subramaniam EswaramoorthyDepartment of Biology, Brookhaven National Laboratory, Upton, New York, USA.
Sébastien Poulain
Rainer Hienerwadel
Nicolas Bremond
Matthew D Sylvester
Yian-Biao Zhang
Catherine Berthomieu
Daniel Van Der Lelie
A Matin
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FRBrookhaven National Laboratory · USStanford University · USInstitute of Environmental Biology and Biotechnology · FRRTI International · US

Funding

MOLECULAR BASIS OF HOST-PARASITE INTERACTIONT32AI007328 · NIAID · STANFORD UNIVERSITY · PI JUSTIN L SONNENBURG · 1987 to 2026
$11.9M
NIAID NIH HHS T32 AI007328
6 · The paper itself

Abstract

The Escherichia coli ChrR enzyme is an obligatory two-electron quinone reductase that has many applications, such as in chromate bioremediation. Its crystal structure, solved at 2.2 Å resolution, shows that it belongs to the flavodoxin superfamily in which flavin mononucleotide (FMN) is firmly anchored to the protein. ChrR crystallized as a tetramer, and size exclusion chromatography showed that this is the oligomeric form that catalyzes chromate reduction. Within the tetramer, the dimers interact by a pair of two hydrogen bond networks, each involving Tyr128 and Glu146 of one dimer and Arg125 and Tyr85 of the other; the latter extends to one of the redox FMN cofactors. Changes in each of these amino acids enhanced chromate reductase activity of the enzyme, showing that this network is centrally involved in chromate reduction.

Indexed as

ChromatesChromatography, GelCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFlavin MononucleotideHydrogen BondingModels, MolecularMutant ProteinsNAD(P)H Dehydrogenase (Quinone)Oxidation-ReductionProtein MultimerizationProtein Structure, QuaternaryChromatesEscherichia coli ProteinsFlavin MononucleotideMutant ProteinsNAD(P)H Dehydrogenase (Quinone)

Identifiers

PMID22558308
PMCPMC3338774
OpenAlexW2078689176

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.