Evidence map›Paper›PMID 29931366›Full record

ArticleFEMS microbiology letters2018

Molecular cloning, expression and biochemical characterization of periplasmic nitrate reductase from Campylobacter jejuni.

Breeanna Mintmier, Jennifer M McGarry, Courtney E Sparacino-Watkins, Joseph Sallmen, Katrin Fischer-Schrader, Axel Magalon, Joseph R McCormick, John F Stolz, Günter Schwarz, Daniel J Bain and 1 more

Open access · greenAbstract read
In one paragraph

Article in FEMS microbiology letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. TheProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. 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
  7. Active Site Characterization of aInorganic chemistry · 2024
    Article
  8. The critical role of a conserved lysine residue in periplasmic nitrate reductase catalyzed reactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  9. Review
  10. Review
  11. Review
  12. Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: a case study with periplasmic nitrate reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  15. Review
  16. Article
  17. Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Review
  18. Influence of Protein Glycosylation onFrontiers in microbiology · 2020
    Article
  19. Proteomics Reveals Multiple Phenotypes Associated withMolecular & cellular proteomics : MCP · 2019
    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

11 authors at 5 institutions in 3 countries.

Breeanna MintmierDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University, Indianapolis, IN 46202, USA.
Jennifer M McGarryDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University, Indianapolis, IN 46202, USA.
Courtney E Sparacino-WatkinsVascular Medicine Institute, University of Pittsburgh School of Medicine, PA 15213, USA.
Joseph SallmenDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
Katrin Fischer-SchraderInstitute for Biochemistry, University of Cologne, Cologne 50674, Germany.
Axel MagalonAix Marseille Université, CNRS, Laboratoire de Chimie Bactérienne (UMR7283), IMM, 13402 Marseille, France.
Joseph R McCormickDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
John F StolzDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
Günter SchwarzInstitute for Biochemistry, University of Cologne, Cologne 50674, Germany.
Daniel J BainDepartment of Geology and Environmental Science, University of Pittsburgh, PA 15260, USA.
Partha BasuDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University, Indianapolis, IN 46202, USA.
Duquesne University · USIndiana University – Purdue University Indianapolis · USUniversity of Cologne · DEUniversity of Pittsburgh · USAix-Marseille Université · FR

Funding

MODELS OF NITRATE REDUCTASES AND RELATED ENZYMESR15GM061555 · NIGMS · DUQUESNE UNIVERSITY · PI BASU, PARTHA · 2000 to 2015
$1.4M
NIGMS NIH HHS R15 GM061555
6 · The paper itself

Abstract

Campylobacter jejuni, a human gastrointestinal pathogen, uses nitrate for growth under microaerophilic conditions using periplasmic nitrate reductase (Nap). The catalytic subunit, NapA, contains two prosthetic groups, an iron sulfur cluster and a molybdenum cofactor. Here we describe the cloning, expression, purification, and Michaelis-Menten kinetics (kcat of 5.91 ± 0.18 s-1 and a KM (nitrate) of 3.40 ± 0.44 μM) in solution using methyl viologen as an electron donor. The data suggest that the high affinity of NapA for nitrate could support growth of C. jejuni on nitrate in the gastrointestinal tract. Site-directed mutagenesis was used and the codon for the molybdenum coordinating cysteine residue has been exchanged for serine. The resulting variant NapA is 4-fold less active than the native enzyme confirming the importance of this residue. The properties of the C. jejuni enzyme reported here represent the first isolation and characterization of an epsilonproteobacterial NapA. Therefore, the fundamental knowledge of Nap has been expanded.

Indexed as

Amino Acid SequenceCloning, MolecularBacterial ProteinsCampylobacter jejuniEnzyme StabilityKineticsModels, MolecularNitrate ReductaseNitratesPeriplasmBacterial ProteinsNitrate ReductaseNitrates

Identifiers

PMID29931366
PMCPMC6692857
OpenAlexW2808946469

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.