Evidence map›Paper›PMID 24809444›Full record

ArticlePloS one2014

Origin and evolution of the sodium -pumping NADH: ubiquinone oxidoreductase.

Adrian Reyes-Prieto, Blanca Barquera, Oscar Juárez

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 97 citations in OpenAlex.

  1. Quinolone inhibitors targetingEuropean journal of medicinal chemistry reports · 2026
    Article
  2. Review
  3. The redox driven NaNature communications · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Inactivation of thebioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. NQR as a target for new antibiotics.Frontiers in microbiology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The respiratory chain ofFrontiers in microbiology · 2024
    Article
  15. Article
  16. Functionality of the NaArchives of microbiology · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. Molecular dynamics modeling of the Vibrio cholera NaMolecular and cellular biochemistry · 2022
    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

3 authors at 2 institutions in 2 countries.

Adrian Reyes-PrietoCanadian Institute for Advanced Research and Biology Department, University of New Brunswick, Fredericton, NB, Canada.
Blanca BarqueraBiology Department, Rensselaer Polytechnic Institute, Troy, New York, United States of America.
Oscar JuárezBiology Department, Rensselaer Polytechnic Institute, Troy, New York, United States of America.
Rensselaer Polytechnic Institute · USUniversity of New Brunswick · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sodium -pumping NADH: ubiquinone oxidoreductase (Na+-NQR) is the main ion pump and the primary entry site for electrons into the respiratory chain of many different types of pathogenic bacteria. This enzymatic complex creates a transmembrane gradient of sodium that is used by the cell to sustain ionic homeostasis, nutrient transport, ATP synthesis, flagellum rotation and other essential processes. Comparative genomics data demonstrate that the nqr operon, which encodes all Na+-NQR subunits, is found in a large variety of bacterial lineages with different habitats and metabolic strategies. Here we studied the distribution, origin and evolution of this enzymatic complex. The molecular phylogenetic analyses and the organizations of the nqr operon indicate that Na+-NQR evolved within the Chlorobi/Bacteroidetes group, after the duplication and subsequent neofunctionalization of the operon that encodes the homolog RNF complex. Subsequently, the nqr operon dispersed through multiple horizontal transfer events to other bacterial lineages such as Chlamydiae, Planctomyces and α, β, γ and δ -proteobacteria. Considering the biochemical properties of the Na+-NQR complex and its physiological role in different bacteria, we propose a detailed scenario to explain the molecular mechanisms that gave rise to its novel redox- dependent sodium -pumping activity. Our model postulates that the evolution of the Na+-NQR complex involved a functional divergence from its RNF homolog, following the duplication of the rnf operon, the loss of the rnfB gene and the recruitment of the reductase subunit of an aromatic monooxygenase.

Indexed as

Evolution, MolecularBacteriaElectron Transport Complex IGene Transfer, HorizontalOperonPhylogenySodium-Potassium-Exchanging ATPaseElectron Transport Complex ISodium-Potassium-Exchanging ATPase

Identifiers

PMID24809444
PMCPMC4014512
OpenAlexW2056721274

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.