Evidence map›Paper›PMID 19805232›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri.

Gargi Kulkarni, Donna M Kridelbaugh, Adam M Guss, William W Metcalf

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
10.3field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 93 citations in OpenAlex.

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  12. Correlation of Key Physiological Properties ofApplied and environmental microbiology · 2021
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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

4 authors at 2 institutions in 3 countries.

Gargi KulkarniDepartment of Microbiology, University of Illinois at Urbana-Champaign, B103 Chemical and Life Science Laboratory, Urbana, IL 61801-3763, USA.
Donna M Kridelbaugh
Adam M Guss
William W Metcalf
University of Illinois Urbana-Champaign · USCenter for Genomic Science · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methanogens use an unusual energy-conserving electron transport chain that involves reduction of a limited number of electron acceptors to methane gas. Previous biochemical studies suggested that the proton-pumping F(420)H(2) dehydrogenase (Fpo) plays a crucial role in this process during growth on methanol. However, Methanosarcina barkeri Delta fpo mutants constructed in this study display no measurable phenotype on this substrate, indicating that Fpo plays a minor role, if any. In contrast, Delta frh mutants lacking the cytoplasmic F(420)-reducing hydrogenase (Frh) are severely affected in their ability to grow and make methane from methanol, and double Delta fpo/Delta frh mutants are completely unable to use this substrate. These data suggest that the preferred electron transport chain involves production of hydrogen gas in the cytoplasm, which then diffuses out of the cell, where it is reoxidized with transfer of electrons into the energy-conserving electron transport chain. This hydrogen-cycling metabolism leads directly to production of a proton motive force that can be used by the cell for ATP synthesis. Nevertheless, M. barkeri does have the flexibility to use the Fpo-dependent electron transport chain when needed, as shown by the poor growth of the Delta frh mutant. Our data suggest that the rapid enzymatic turnover of hydrogenases may allow a competitive advantage via faster growth rates in this freshwater organism. The mutant analysis also confirms the proposed role of Frh in growth on hydrogen/carbon dioxide and suggests that either Frh or Fpo is needed for aceticlastic growth of M. barkeri.

Indexed as

Electron TransportAdenosine TriphosphateArchaeal ProteinsElectron Transport Chain Complex ProteinsEnergy MetabolismGenes, ArchaealGenome, ArchaealHydrogenMethaneMethanosarcina barkeriModels, BiologicalMutationOxidoreductasesPhenazinesProton-Motive ForceAdenosine TriphosphateArchaeal Proteinscoenzyme F420 hydrogenaseElectron Transport Chain Complex ProteinsF420H2 dehydrogenaseHydrogenMethanemethanophenazineOxidoreductasesPhenazines

Identifiers

PMID19805232
PMCPMC2747218
OpenAlexW2139066998

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.