Evidence map›Paper›PMID 24474405›Full record

ArticleCurrent microbiology2014

A Rhizobium selenitireducens protein showing selenite reductase activity.

W J Hunter

Abstract read
PubMed Publisher
In one paragraph

Article in Current microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Non-nodulatingISME communications · 2026
    Article
  5. Article
  6. Article
  7. Selenite bioreduction with concomitant green synthesis of selenium nanoparticles by a selenite resistant EPS and siderophore producing terrestrial bacterium.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Fungal formation of selenium and tellurium nanoparticles.Applied microbiology and biotechnology · 2019
    Article
  14. Selenium Nanoparticle Synthesized byInternational journal of molecular sciences · 2018
    Article
  15. Selenite Reduction and the Biogenesis of Selenium Nanoparticles byInternational journal of molecular sciences · 2018
    Article
  16. High-quality-draft genomic sequence ofStandards in genomic sciences · 2017
    Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

W J HunterUnited States Department of Agriculture-Agricultural Research Service, 2150-D Centre Avenue, Fort Collins, CO, 80526-8119, USA, william.hunter@ars.usda.gov.
United States Department of Agriculture · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biobarriers remove, via precipitation, the metalloid selenite (SeO₃⁻²) from groundwater; a process that involves the biological reduction of soluble SeO₃⁻² to insoluble elemental red selenium (Se⁰). The enzymes associated with this reduction process are poorly understood. In Rhizobium selenitireducens at least two enzymes are potentially involved; one, a nitrite reductase reduces SeO₃⁻² to Se⁰ but another protein may also be involved which is investigated in this study. Proteins from R. selenitireducens cells were precipitated with ammonium sulfate and run on native electrophoresis gels. When these gels were incubated with NADH and SeO₃⁻² a band of precipitated Se⁰ developed signifying the presence of a SeO₃⁻² reducing protein. Bands were cut from the gel and analyzed for peptides via LCMSMS. The amino acid sequences associated with the bands indicated the presence of an NADH:flavin oxidoreductase that resembles YP_001326930 from Sinorhizobium medicae. The protein is part of a protein family termed old-yellow-enzymes (OYE) that contain a flavin binding domain. OYE enzymes are often involved in protecting cells from oxidative stress and, due in part to an active site that has a highly accessible binding pocket, are generally active on a wide range of substrates. This report is the first of an OYE enzyme being involved in SeO₃⁻² reduction.

Indexed as

Bacterial ProteinsChemical PrecipitationChromatography, LiquidElectrophoresisFMN ReductaseNADOxidation-ReductionSelenious AcidSequence Homology, Amino AcidSinorhizobiumTandem Mass SpectrometryBacterial ProteinsFMN ReductaseNADSelenious Acid

Identifiers

PMID24474405
OpenAlexW2107920134

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.