Evidence map›Paper›PMID 28671181›Full record

ArticleNature communications2017

Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer.

Cindy Kunze, Martin Bommer, Wilfred R Hagen, Marie Uksa, Holger Dobbek, Torsten Schubert, Gabriele Diekert

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Mechanism of FThe journal of physical chemistry. B · 2026
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  5. Review
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  15. Chlorination of arenes via the degradation of toxic chlorophenols.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Biocatalytic Reduction Reactions from a Chemist's Perspective.Angewandte Chemie (International ed. in English) · 2021
    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

7 authors at 3 institutions in 2 countries.

Cindy KunzeDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Philosophenweg 12, Jena D-07743, Germany.
Martin BommerStructural Biology/Biochemistry, Institute of Biology, Humboldt Universität zu Berlin, Philippstrasse 13, Berlin D-10115, Germany.
Wilfred R HagenDepartment of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, van der Maasweg 9, Delft 2629HZ, The Netherlands.
Marie UksaDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Philosophenweg 12, Jena D-07743, Germany.
Holger DobbekStructural Biology/Biochemistry, Institute of Biology, Humboldt Universität zu Berlin, Philippstrasse 13, Berlin D-10115, Germany.
Torsten SchubertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Philosophenweg 12, Jena D-07743, Germany.ORCID 0000-0002-6569-1194
Gabriele DiekertDepartment of Applied and Ecological Microbiology, Institute of Microbiology, Friedrich Schiller University, Philosophenweg 12, Jena D-07743, Germany.
Friedrich Schiller University Jena · DEHumboldt-Universität zu Berlin · DEDelft University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The capacity of metal-containing porphyrinoids to mediate reductive dehalogenation is implemented in cobamide-containing reductive dehalogenases (RDases), which serve as terminal reductases in organohalide-respiring microbes. RDases allow for the exploitation of halogenated compounds as electron acceptors. Their reaction mechanism is under debate. Here we report on substrate-enzyme interactions in a tetrachloroethene RDase (PceA) that also converts aryl halides. The shape of PceA's highly apolar active site directs binding of bromophenols at some distance from the cobalt and with the hydroxyl substituent towards the metal. A close cobalt-substrate interaction is not observed by electron paramagnetic resonance spectroscopy. Nonetheless, a halogen substituent para to the hydroxyl group is reductively eliminated and the path of the leaving halide is traced in the structure. Based on these findings, an enzymatic mechanism relying on a long-range electron transfer is concluded, which is without parallel in vitamin B

Indexed as

Bacterial ProteinsCampylobacteraceaeCatalysisCatalytic DomainCobamidesElectron Spin Resonance SpectroscopyElectron TransportHalogenationOxidoreductasesVitamin B 12Bacterial ProteinsCobamidesOxidoreductasesVitamin B 12

Identifiers

PMID28671181
PMCPMC5500849
OpenAlexW2729040759

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.