Evidence map›Paper›PMID 30850546›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Energy conservation by a hydrogenase-dependent chemiosmotic mechanism in an ancient metabolic pathway.

Marie Charlotte Schoelmerich, Volker Müller

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
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

51 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  6. Frontiers in microbiology · 2026
    Article
  7. Article
  8. Article
  9. Article
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  11. Isolation and characterization ofInternational journal of systematic and evolutionary microbiology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Extremophiles in a changing world.Extremophiles : life under extreme conditions · 2024
    Review
  17. Article
  18. Ferredoxin reduction by hydrogen with iron functions as an evolutionary precursor of flavin-based electron bifurcation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Review
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.

Marie Charlotte SchoelmerichMolecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt/Main, 60438 Frankfurt, Germany.ORCID 0000-0001-7679-0043
Volker MüllerMolecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt/Main, 60438 Frankfurt, Germany vmueller@bio.uni-frankfurt.de.ORCID 0000-0001-7955-5508
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ancient reductive acetyl-CoA pathway is employed by acetogenic bacteria to form acetate from inorganic energy sources. Since the central pathway does not gain net ATP by substrate-level phosphorylation, chemolithoautotrophic growth relies on the additional formation of ATP via a chemiosmotic mechanism. Genome analyses indicated that some acetogens only have an energy-converting, ion-translocating hydrogenase (Ech) as a potential respiratory enzyme. Although the Ech-encoding genes are widely distributed in nature, the proposed function of Ech as an ion-translocating chemiosmotic coupling site has neither been demonstrated in bacteria nor has it been demonstrated that it can be the only energetic coupling sites in microorganisms that depend on a chemiosmotic mechanism for energy conservation. Here, we show that the Ech complex of the thermophilic acetogenic bacterium

Indexed as

Biochemical PhenomenaMetabolic Networks and PathwaysAdenosine TriphosphateAldehyde OxidoreductasesCarbon CycleCarbon MonoxideCell MembraneHydrogenMultienzyme ComplexesMultigene FamilyOxidation-ReductionOxidoreductasesProton-Motive ForceSecretory VesiclesSodiumThermoanaerobacterAdenosine TriphosphateAldehyde OxidoreductasesCarbon Monoxidecarbon monoxide dehydrogenaseEch hydrogenaseHydrogenMultienzyme ComplexesOxidoreductasesSodiumacetogenesisbioenergeticschemiosmosisenergy-converting hydrogenaserespiratory mechanism

Identifiers

PMID30850546
PMCPMC6442639
OpenAlexW2921348589

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.