Evidence map›Paper›PMID 41248713›Full record

ArticleThe Journal of biological chemistry2025

Structure and substrate promiscuity of Campylobacter jejuni periplasmic nitrate reductase (Nap) and phylogenetic analysis of Nap homologs.

Nitai C Giri, Trung Thach, KanagaVijayan Dhanabalan, Mintare Cesiunaite, Manohar Radhakrishnan, Lahiru Wedasingha, Nicholas Manicke, Michael Wells, Maciej Szaleniec, Ramaswamy Subramanian and 1 more

Abstract read
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In one paragraph

Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Structure and function of periplasmic nitrate reductase.Biochemical Society transactions · 2026
    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

11 authors.

Nitai C GiriDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Trung ThachDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
KanagaVijayan DhanabalanDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
Mintare CesiunaiteDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Manohar RadhakrishnanDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Lahiru WedasinghaDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Nicholas ManickeDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Michael WellsSchool of Biological Sciences, Louisiana Tech University, Ruston, Louisiana, USA.
Maciej SzaleniecJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Kraków, Poland. Electronic address: maciej.szaleniec@ikifp.edu.pl.
Ramaswamy SubramanianDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA. Electronic address: subram68@purdue.edu.
Partha BasuDepartment of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA. Electronic address: basup@iu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Periplasmic nitrate reductase NapA is a member of the DMSO reductase (DMSOR) superfamily, which catalyzes the reduction of nitrate to nitrite. Campylobacter jejuni NapA (CjNapA) is notably larger compared to other structurally characterized NapA. Herein, we present the cryo-EM structure of CjNapA, the first of its kind from any ε-proteobacteria, revealing three lysine-rich insertions that could affect the substrate channel, potentially enhancing the affinity towards nitrate and other anionic substrates. Here, we report that wild-type CjNapA and NapA-C176D variants can reduce chlorate, perchlorate, and nitrate. However, the perchlorate and chlorate reductions by the CjNapA C176D variant are considerably slower, even though the perchlorate reductase has an Asp coordination to Mo. Molecular Dynamics (MD) simulations were performed to investigate the impact of the C176D mutation on substrate affinity and protein flexibility. Structural and kinetic comparisons with perchlorate reductase support evolutionary tuning for a desired function. Finally, structural comparisons with other structurally characterized NapAs also suggest the role of proximal pterin in CjNapA in electron transfer to the Mo center.

Indexed as

Bacterial ProteinsCampylobacter jejuniNitrate ReductasePeriplasmCryoelectron MicroscopyKineticsMolecular Dynamics SimulationNitratesPerchloratesPhylogenySubstrate SpecificityBacterial ProteinsNitrate ReductaseNitratesperchloratePerchloratescryo-EMmolybdenum enzymesperiplasmic nitrate reductasestructure-function

Identifiers

PMID41248713
PMCPMC12769810

What Socratic holds

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LicenceCC BY
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Registered trials

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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 Socratic graph.