Evidence map›Paper›PMID 25368299›Full record

ArticleJournal of bacteriology2015

Physiology and bioenergetics of [NiFe]-hydrogenase 2-catalyzed H2-consuming and H2-producing reactions in Escherichia coli.

Constanze Pinske, Monique Jaroschinsky, Sabine Linek, Ciarán L Kelly, Frank Sargent, R Gary Sawers

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 71 citations in OpenAlex.

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  7. Frontiers in microbiology · 2023
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  14. Review
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  20. The structure of hydrogenase-2 fromThe Biochemical journal · 2018
    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

6 authors at 2 institutions in 2 countries.

Constanze PinskeDivision of Molecular Microbiology, University of Dundee, College of Life Sciences, Dundee, Scotland, United Kingdom.
Monique JaroschinskyInstitute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Sabine LinekInstitute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Ciarán L KellyDivision of Molecular Microbiology, University of Dundee, College of Life Sciences, Dundee, Scotland, United Kingdom.
Frank SargentDivision of Molecular Microbiology, University of Dundee, College of Life Sciences, Dundee, Scotland, United Kingdom f.sargent@dundee.ac.uk gary.sawers@mikrobiologie.uni-halle.de.
R Gary SawersInstitute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany f.sargent@dundee.ac.uk gary.sawers@mikrobiologie.uni-halle.de.
Martin Luther University Halle-Wittenberg · DEUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I02008X/1Biotechnology and Biological Sciences Research Council BB/L008521/1
6 · The paper itself

Abstract

Escherichia coli uptake hydrogenase 2 (Hyd-2) catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 synthesis is strongly upregulated during growth on glycerol or on glycerol-fumarate. Membrane-associated Hyd-2 is an unusual heterotetrameric [NiFe]-hydrogenase that lacks a typical cytochrome b membrane anchor subunit, which transfers electrons to the quinone pool. Instead, Hyd-2 has an additional electron transfer subunit, termed HybA, with four predicted iron-sulfur clusters. Here, we examined the physiological role of the HybA subunit. During respiratory growth with glycerol and fumarate, Hyd-2 used menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction. HybA was essential for electron transfer from Hyd-2 to MQ/DMQ. H2 evolution catalyzed by Hyd-2 during fermentation of glycerol in the presence of Casamino Acids or in a fumarate reductase-negative strain growing with glycerol-fumarate was also shown to be dependent on both HybA and MQ/DMQ. The uncoupler carbonyl cyanide m-chlorophenylhydrazone (CCCP) inhibited Hyd-2-dependent H2 evolution from glycerol, indicating the requirement for a proton gradient. In contrast, CCCP failed to inhibit H2-coupled fumarate reduction. Although a Hyd-2 enzyme lacking HybA could not catalyze Hyd-2-dependent H2 oxidation or H2 evolution in whole cells, reversible H2-dependent reduction of viologen dyes still occurred. Finally, hydrogen-dependent dye reduction by Hyd-2 was reversibly inhibited in extracts derived from cells grown in H2 evolution mode. Our findings suggest that Hyd-2 switches between H2-consuming and H2-producing modes in response to the redox status of the quinone pool. Hyd-2-dependent H2 evolution from glycerol requires reverse electron transport.

Indexed as

Carbonyl Cyanide m-Chlorophenyl HydrazoneEscherichia coliEscherichia coli ProteinsHydrogenHydrogenaseCarbonyl Cyanide m-Chlorophenyl HydrazoneEscherichia coli ProteinsHydrogenHydrogenasenickel-iron hydrogenase

Identifiers

PMID25368299
PMCPMC4272588
OpenAlexW2073628273

What OpenQuestion holds

Textmetadata
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Registered trials

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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.