Evidence map›Paper›PMID 27139710›Full record

ArticleMicrobiologyOpen2016

Exploring the directionality of Escherichia coli formate hydrogenlyase: a membrane-bound enzyme capable of fixing carbon dioxide to organic acid.

Constanze Pinske, Frank Sargent

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

32 citing papers in PubMed, 66 citations in OpenAlex.

  1. Genetic dissection of formate hydrogenlyase-2 function: a metalloenzyme involved in bacterial hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. NADPApplied and environmental microbiology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Hydrogen-fueled COFrontiers in bioengineering and biotechnology · 2022
    Article
  11. HThe ISME journal · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Formate-Dependent Heterodisulfide Reduction in aApplied and environmental microbiology · 2021
    Article
  16. Article
  17. Article
  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

2 authors at 1 institution in 1 country.

Constanze PinskeDivision of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, Scotland, DD1 5EH, United Kingdom.
Frank SargentDivision of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, Scotland, DD1 5EH, United Kingdom. f.sargent@dundee.ac.uk.ORCID http://orcid.org/0000-0002-6841-3624
University of Dundee · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During mixed-acid fermentation Escherichia coli produces formate, which is initially excreted out the cell. Accumulation of formate, and dropping extracellular pH, leads to biosynthesis of the formate hydrogenlyase (FHL) complex. FHL consists of membrane and soluble domains anchored within the inner membrane. The soluble domain comprises a [NiFe] hydrogenase and a formate dehydrogenase that link formate oxidation directly to proton reduction with the release of CO

Indexed as

Amino Acid SequenceCarbon DioxideEscherichia coliEscherichia coli ProteinsFermentationFormate DehydrogenasesFormatesHydrogenaseMembrane ProteinsMultienzyme ComplexesOxidation-ReductionProtein Structure, TertiaryCarbon DioxideEscherichia coli ProteinsFormate Dehydrogenasesformate hydrogenlyaseFormatesformic acidHydrogenaseMembrane ProteinsMultienzyme Complexesnickel-iron hydrogenasebacterial hydrogen metabolismformate chemosynthesisformate dehydrogenaseformate hydrogenlyase[NiFe] hydrogenasesite-directed mutagenesis

Identifiers

PMID27139710
PMCPMC5061711
OpenAlexW2345415351

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.