Evidence map›Paper›PMID 26362109›Full record

ReviewProtein science : a publication of the Protein Society2015

Structural and mechanistic insights on nitrate reductases.

Catarina Coelho, Maria João Romão

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

32 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
  2. Article
  3. Structure and function of periplasmic nitrate reductase.Biochemical Society transactions · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Nitrate-Nitrite Interplay in the Nitrogen Biocycle.Molecules (Basel, Switzerland) · 2025
    Review
  11. Article
  12. Article
  13. Insights into periplasmic nitrate reductase function under single turnover.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  14. Stable isotopic signature of dissimilatory nitrate reduction is robust against enzyme mutation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Microorganisms · 2023
    Review
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

2 authors at 1 institution in 1 country.

Catarina CoelhoDepartamento de Química, Faculdade de Ciências e Tecnologia, UCIBIO@REQUIMTE, Universidade Nova de Lisboa, Caparica, 2829-516, Portugal.ORCID http://orcid.org/0000-0003-1852-5406
Maria João RomãoDepartamento de Química, Faculdade de Ciências e Tecnologia, UCIBIO@REQUIMTE, Universidade Nova de Lisboa, Caparica, 2829-516, Portugal.
Rede de Química e Tecnologia · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrate reductases (NR) belong to the DMSO reductase family of Mo-containing enzymes and perform key roles in the metabolism of the nitrogen cycle, reducing nitrate to nitrite. Due to variable cell location, structure and function, they have been divided into periplasmic (Nap), cytoplasmic, and membrane-bound (Nar) nitrate reductases. The first crystal structure obtained for a NR was that of the monomeric NapA from Desulfovibrio desulfuricans in 1999. Since then several new crystal structures were solved providing novel insights that led to the revision of the commonly accepted reaction mechanism for periplasmic nitrate reductases. The two crystal structures available for the NarGHI protein are from the same organism (Escherichia coli) and the combination with electrochemical and spectroscopic studies also lead to the proposal of a reaction mechanism for this group of enzymes. Here we present an overview on the current advances in structural and functional aspects of bacterial nitrate reductases, focusing on the mechanistic implications drawn from the crystallographic data.

Indexed as

BacteriaBacterial ProteinsCatalytic DomainCell MembraneCrystallography, X-RayCytoplasmModels, MolecularNitrate ReductasePeriplasmBacterial ProteinsNitrate Reductasecrystal structureDMSO reductase familyenzymatic mechanismmembrane-bound nitrate reductasemolybdenum enzymesnitrogen cycleperiplasmic nitrate reductase

Identifiers

PMID26362109
PMCPMC4815237
OpenAlexW2166125203

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.