Evidence map›Paper›PMID 27735784›Full record

ReviewEcoSal Plus2016

Anaerobic Formate and Hydrogen Metabolism.

Constanze Pinske, R Gary Sawers

Abstract readReview
In one paragraph

Review in EcoSal Plus, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  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
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  7. Nitric Oxide Inhibition of Glycyl Radical Enzymes and Their Activases.Journal of the American Chemical Society · 2025
    Article
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  9. Review
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  17. CJournal of bacteriology · 2022
    Review
  18. HyfF subunit of hydrogenase 4 is crucial for regulating FJournal of bioenergetics and biomembranes · 2022
    Article
  19. Hydrogen production in the presence of oxygen byMicrobiology (Reading, England) · 2022
    Article
  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.

Constanze PinskeInstitute of Biology/Microbiology, Martin Luther University, Halle-Wittenberg, 06120 Halle, Germany.
R Gary SawersInstitute of Biology/Microbiology, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous recent developments in the biochemistry, molecular biology, and physiology of formate and H2 metabolism and of the [NiFe]-hydrogenase (Hyd) cofactor biosynthetic machinery are highlighted. Formate export and import by the aquaporin-like pentameric formate channel FocA is governed by interaction with pyruvate formate-lyase, the enzyme that generates formate. Formate is disproportionated by the reversible formate hydrogenlyase (FHL) complex, which has been isolated, allowing biochemical dissection of evolutionary parallels with complex I of the respiratory chain. A recently identified sulfido-ligand attached to Mo in the active site of formate dehydrogenases led to the proposal of a modified catalytic mechanism. Structural analysis of the homologous, H2-oxidizing Hyd-1 and Hyd-5 identified a novel proximal [4Fe-3S] cluster in the small subunit involved in conferring oxygen tolerance to the enzymes. Synthesis of Salmonella Typhimurium Hyd-5 occurs aerobically, which is novel for an enterobacterial Hyd. The O2-sensitive Hyd-2 enzyme has been shown to be reversible: it presumably acts as a conformational proton pump in the H2-oxidizing mode and is capable of coupling reverse electron transport to drive H2 release. The structural characterization of all the Hyp maturation proteins has given new impulse to studies on the biosynthesis of the Fe(CN)2CO moiety of the [NiFe] cofactor. It is synthesized on a Hyp-scaffold complex, mainly comprising HypC and HypD, before insertion into the apo-large subunit. Finally, clear evidence now exists indicating that Escherichia coli can mature Hyd enzymes differentially, depending on metal ion availability and the prevailing metabolic state. Notably, Hyd-3 of the FHL complex takes precedence over the H2-oxidizing enzymes.

Indexed as

AcetyltransferasesAnaerobiosisBiocatalysisElectron TransportEscherichia coliEscherichia coli ProteinsFormate DehydrogenasesFormatesHydrogenHydrogenaseMultienzyme ComplexesOxidation-ReductionSalmonella typhimuriumAcetyltransferasesEscherichia coli Proteinsformate C-acetyltransferaseFormate Dehydrogenasesformate hydrogenlyaseFormatesHydrogenHydrogenaseMultienzyme Complexesnickel-iron hydrogenase

Identifiers

PMID27735784
PMCPMC11575713

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.