Evidence map›Paper›PMID 36104349›Full record

ArticleNature communications2022

Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.

Ralf Steinhilper, Gabriele Höff, Johann Heider, Bonnie J Murphy

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Trial
  2. Article
  3. 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
  4. Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026
    Article
  5. Semiartificial COChemical reviews · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Frontiers in microbiology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Ralf SteinhilperRedox and Metalloprotein Research Group, Max Planck Institute of Biophysics, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-4564-8348
Gabriele HöffDepartment of Biology, Laboratory for Microbial Biochemistry, Philipps University Marburg, 35043, Marburg, Germany.
Johann HeiderDepartment of Biology, Laboratory for Microbial Biochemistry, Philipps University Marburg, 35043, Marburg, Germany.
Bonnie J MurphyRedox and Metalloprotein Research Group, Max Planck Institute of Biophysics, 60438, Frankfurt am Main, Germany. bonnie.murphy@biophys.mpg.de.ORCID http://orcid.org/0000-0001-6341-9368
Max Planck Institute of Biophysics · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H

Indexed as

Escherichia coli ProteinsHydrogenaseEscherichia coliFormate DehydrogenasesHydrogenEscherichia coli ProteinsFormate DehydrogenasesHydrogenHydrogenase

Identifiers

PMID36104349
PMCPMC9474812
OpenAlexW4295763067

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.