Evidence map›Paper›PMID 29364838›Full record

ArticleMolecules (Basel, Switzerland)2018

Informing Efforts to Develop Nitroreductase for Amine Production.

Anne-Frances Miller, Jonathan T Park, Kyle L Ferguson, Warintra Pitsawong, Andreas S Bommarius

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Real-Time Detection of Reduced Nitroreductase with a Reversible Fluorescent Probe.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Targeted Delivery of Persulfides to the Gut: Effects on the Microbiome.Angewandte Chemie (International ed. in English) · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Special Issue: Flavoenzymes.Molecules (Basel, Switzerland) · 2018
    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

5 authors at 2 institutions in 1 country.

Anne-Frances MillerDepartment of Chemistry, University of Kentucky, Lexington, KY 40506-0055, USA. afmill3r2@gmail.com.
Jonathan T ParkSchool of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0100, USA. jpark5009@gmail.com.
Kyle L FergusonSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0100, USA. k.ferge@gmail.com.
Warintra PitsawongDepartment of Chemistry, University of Kentucky, Lexington, KY 40506-0055, USA. warintra@brandeis.edu.
Andreas S BommariusSchool of Chemical and Biomolecular Engineering, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0100, USA. andreas.bommarius@chbe.gatech.edu.
Georgia Institute of Technology · USUniversity of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitroreductases (NRs) hold promise for converting nitroaromatics to aromatic amines. Nitroaromatic reduction rate increases with Hammett substituent constant for NRs from two different subgroups, confirming substrate identity as a key determinant of reactivity. Amine yields were low, but compounds yielding amines tend to have a large π system and electron withdrawing substituents. Therefore, we also assessed the prospects of varying the enzyme. Several different subgroups of NRs include members able to produce aromatic amines. Comparison of four NR subgroups shows that they provide contrasting substrate binding cavities with distinct constraints on substrate position relative to the flavin. The unique architecture of the NR dimer produces an enormous contact area which we propose provides the stabilization needed to offset the costs of insertion of the active sites between the monomers. Thus, we propose that the functional diversity included in the NR superfamily stems from the chemical versatility of the flavin cofactor in conjunction with a structure that permits tremendous active site variability. These complementary properties make NRs exceptionally promising enzymes for development for biocatalysis in prodrug activation and conversion of nitroaromatics to valuable aromatic amines. We provide a framework for identifying NRs and substrates with the greatest potential to advance.

Indexed as

FermentationAminesBinding SitesBiosynthetic PathwaysModels, MolecularMolecular ConformationMolecular StructureNADNitroreductasesOxidation-ReductionProtein BindingStructure-Activity RelationshipSubstrate SpecificityAminesNADNitroreductasesdomain-swapped dimerenzyme-aided synthesisflavinflavoenzymeintertwined dimernitroreductasestructure-activitystructure-function

Identifiers

PMID29364838
PMCPMC6017928
OpenAlexW2794327236

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.