Evidence map›Paper›PMID 42206606›Full record

ReviewBiochemical Society transactions2026

Structure and function of periplasmic nitrate reductase.

Chanakarn Mongkonpruthangkoon, Nitai C Giri, Partha Basu

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biochemical Society transactions, 2026. 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. 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

3 authors.

Chanakarn MongkonpruthangkoonDepartment of Chemistry and Chemical Biology, Indiana University Indianapolis, Indianapolis, IN 46202, U.S.A.ORCID 0009-0008-5807-9600
Nitai C GiriDepartment of Chemistry and Chemical Biology, Indiana University Indianapolis, Indianapolis, IN 46202, U.S.A.ORCID 0000-0002-0476-840X
Partha BasuDepartment of Chemistry and Chemical Biology, Indiana University Indianapolis, Indianapolis, IN 46202, U.S.A.ORCID 0000-0002-1232-418X

Funding

HHS | National Institutes of Health (NIH) GM 139064National Science Foundation (NSF) CHE 2003752
6 · The paper itself

Abstract

Nitrate reductases are molybdenum cofactor (Moco)-containing enzymes that reduce nitrate to nitrite, the first step in assimilatory and dissimilatory nitrate reduction to ammonia, and in denitrification. Nitrate reductases are divided into four groups; this review will focus on periplasmic nitrate reductase (Nap), discussing the available structures of NapA in the context of other members of the DMSO reductase family. The mechanism and the roles of a specific amino acid residue are also discussed.

Indexed as

Nitrate ReductasePeriplasmCoenzymesIron-Sulfur ProteinsMetalloproteinsModels, MolecularMolybdenum CofactorsNitratesOxidoreductasesProtein ConformationPteridinesCoenzymesdimethyl sulfoxide reductaseIron-Sulfur ProteinsMetalloproteinsMolybdenum CofactorsmolybdopterinNitrate ReductaseNitratesOxidoreductasesPteridinesDMSO reductase familymechanismmolybdenum cofactornitrate reductaseoperon structurepterin conformation

Identifiers

PMID42206606
PMCPMC13223375

What OpenQuestion holds

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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.