Evidence map›Paper›PMID 25157147›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Bacterial formate hydrogenlyase complex.

Jennifer S McDowall, Bonnie J Murphy, Michael Haumann, Tracy Palmer, Fraser A Armstrong, Frank Sargent

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
6.2field-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

124 citing papers in PubMed, 265 citations in OpenAlex.

  1. Article
  2. 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
  3. Semiartificial COChemical reviews · 2026
    Review
  4. Article
  5. Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  6. Native HNature chemistry · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. The Adaptations ofThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2026
    Article
  11. Frontiers in microbiology · 2026
    Article
  12. Sustainable co-production of 1,3-PDO, ethanol and HFrontiers in bioengineering and biotechnology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

64 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Jennifer S McDowallDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland;
Bonnie J MurphyInorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QR, United Kingdom; and.
Michael HaumannInstitut für Experimentalphysik, Freie Universität Berlin, 14195 Berlin, Germany.
Tracy PalmerDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland;
Fraser A ArmstrongInorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QR, United Kingdom; and.
Frank SargentDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland; f.sargent@dundee.ac.uk.
University of Dundee · GBUniversity of Oxford · GBFreie Universität Berlin · DE

Funding

Biotechnology and Biological Sciences Research Council BB/H001190/1Biotechnology and Biological Sciences Research Council BB/H003878-1Biotechnology and Biological Sciences Research Council BB/H003878/1Biotechnology and Biological Sciences Research Council BB/I02008X/1Biotechnology and Biological Sciences Research Council BB/I022309-1
6 · The paper itself

Abstract

Under anaerobic conditions, Escherichia coli can carry out a mixed-acid fermentation that ultimately produces molecular hydrogen. The enzyme directly responsible for hydrogen production is the membrane-bound formate hydrogenlyase (FHL) complex, which links formate oxidation to proton reduction and has evolutionary links to Complex I, the NADH:quinone oxidoreductase. Although the genetics, maturation, and some biochemistry of FHL are understood, the protein complex has never been isolated in an intact form to allow biochemical analysis. In this work, genetic tools are reported that allow the facile isolation of FHL in a single chromatographic step. The core complex is shown to comprise HycE (a [NiFe] hydrogenase component termed Hyd-3), FdhF (the molybdenum-dependent formate dehydrogenase-H), and three iron-sulfur proteins: HycB, HycF, and HycG. A proportion of this core complex remains associated with HycC and HycD, which are polytopic integral membrane proteins believed to anchor the core complex to the cytoplasmic side of the membrane. As isolated, the FHL complex retains formate hydrogenlyase activity in vitro. Protein film electrochemistry experiments on Hyd-3 demonstrate that it has a unique ability among [NiFe] hydrogenases to catalyze production of H2 even at high partial pressures of H2. Understanding and harnessing the activity of the FHL complex is critical to advancing future biohydrogen research efforts.

Indexed as

CatalysisEscherichia coliEscherichia coli ProteinsFormate DehydrogenasesHydrogenHydrogenaseIron-Sulfur ProteinsMultienzyme ComplexesMultiprotein ComplexesEscherichia coli ProteinsFormate Dehydrogenasesformate hydrogenlyasehycE protein, E coliHydrogenHydrogenaseIron-Sulfur ProteinsMultienzyme ComplexesMultiprotein Complexesbacterial hydrogen metabolismPFE

Identifiers

PMID25157147
PMCPMC4183296
OpenAlexW2058878931

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.