Evidence map›Paper›PMID 24814779›Full record

ArticleApplied and environmental microbiology2014

Functional heterologous production of reductive dehalogenases from Desulfitobacterium hafniense strains.

Anita Mac Nelly, Marco Kai, Aleš Svatoš, Gabriele Diekert, Torsten Schubert

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Developing anApplied and environmental microbiology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Heterologous Expression of ActiveApplied and environmental microbiology · 2022
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Microbial degradation of chloroethenes: a review.Environmental science and pollution research international · 2017
    Review
  17. Review
  18. Article
  19. Review
  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

5 authors at 2 institutions in 1 country.

Anita Mac NellyDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany.
Marco KaiResearch Group Mass Spectrometry, Max Planck Institute for Chemical Ecology, Jena, Germany.
Aleš SvatošResearch Group Mass Spectrometry, Max Planck Institute for Chemical Ecology, Jena, Germany.
Gabriele DiekertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany.
Torsten SchubertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Jena, Germany torsten.schubert@uni-jena.de.
Friedrich Schiller University Jena · DEMax Planck Institute for Chemical Ecology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The anaerobic dehalogenation of organohalides is catalyzed by the reductive dehalogenase (RdhA) enzymes produced in phylogenetically diverse bacteria. These enzymes contain a cobamide cofactor at the active site and two iron-sulfur clusters. In this study, the tetrachloroethene (PCE) reductive dehalogenase (PceA) of the Gram-positive Desulfitobacterium hafniense strain Y51 was produced in a catalytically active form in the nondechlorinating, cobamide-producing bacterium Shimwellia blattae (ATCC 33430), a Gram-negative gammaproteobacterium. The formation of recombinant catalytically active PceA enzyme was significantly enhanced when its dedicated PceT chaperone was coproduced and when 5,6-dimethylbenzimidazole and hydroxocobalamin were added to the S. blattae cultures. The experiments were extended to D. hafniense DCB-2, a reductively dehalogenating bacterium harboring multiple rdhA genes. To elucidate the substrate spectrum of the rdhA3 gene product of this organism, the recombinant enzyme was tested for the conversion of different dichlorophenols (DCP) in crude extracts of an RdhA3-producing S. blattae strain. 3,5-DCP, 2,3-DCP, and 2,4-DCP, but not 2,6-DCP and 3,4-DCP, were reductively dechlorinated by the recombinant RdhA3. In addition, this enzyme dechlorinated PCE to trichloroethene at low rates.

Indexed as

Allyl CompoundsBacterial ProteinsBenzimidazolesCatalysisChlorophenolsCloning, MolecularCobamidesCulture MediaDesulfitobacteriumDNA, BacterialGammaproteobacteriaHalogenationHydrocarbons, ChlorinatedHydroxocobalaminOxidoreductasesPlasmids2,3-dichloro-1-propene3,5-dichlorophenol5,6-dimethylbenzimidazoleAllyl CompoundsBacterial ProteinsBenzimidazolesChlorophenolsCobamidesCulture MediaDNA, BacterialHydrocarbons, ChlorinatedHydroxocobalaminOxidoreductasessulfonated 2,4-dichlorophenoltetrachloroethene dehalogenaseTrichloroethylene

Identifiers

PMID24814779
PMCPMC4068680
OpenAlexW2114772522

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.