Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Hydrogenase activity and proton-motive force generation by Escherichia coli during glycerol fermentation.

Journal of bioenergetics and biomembranes - 1 Jun 2013

Trchounian Karen, Blbulyan Syuzanna, Trchounian Armen

Abstract excerpt

Proton motive force (Δp) generation by Escherichia coli wild type cells during glycerol fermentation was first studied. Its two components, electrical-the membrane potential (∆φ) and chemical-the pH transmembrane gradient (ΔpH), were established and the effects of external pH (pHex) were determined. Intracellular pH was 7.0 and 6.0 and lower than pHex at pH 7.5 and 6.5, respectively; and it was higher than pHex...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glucose

Share to Glycerol

Share to Hydrogen-Ion Concentration

Share to Hydrogenase

Share to Proton-Motive Force

Share to Proton-Translocating ATPases

Source

Identifiers

PMID: 23271421
DOI: 10.1007/s10863-012-9498-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hydrogenase activity and proton-motive force generation by Escherichia coli during glycerol fermentation.PMID 23271421Read ↗

Impact of membrane-associated hydrogenases on the F₀F₁-ATPase in Escherichia coli during glycerol and mixed carbon fermentation: ATPase activity and its inhibition by N,N'-dicyclohexylcarbodiimide in the mutants lacking hydrogenases.Semantic proximity Read ↗

FhlA-mediated regulation of proton transport and energy transduction in Escherichia coli at acidic pH.Semantic proximity Read ↗

Glucose concentration is determinant for the functioning of hydrogenase 1 and hydrogenase 2 in regulating the proton and potassium fluxes in Escherichia coli at pH 7.5.Semantic proximity Read ↗

Transcriptional control of hydrogen production during mixed carbon fermentation by hydrogenases 4 (hyf) and 3 (hyc) in Escherichia coli.Semantic proximity Read ↗

Influence of C4 -Dcu transporters on hydrogenase and formate dehydrogenase activities in stationary phase-grown fermenting Escherichia coli.Semantic proximity Read ↗

Formate increases the F0F1-ATPase activity in Escherichia coli growing on glucose under anaerobic conditions at slightly alkaline pH.Semantic proximity Read ↗

[Membrane proton conductivity and energy-dependent fluxes of hydrogen ions in bacteria Enterococcus hirae grown in media with different pH values].Semantic proximity Read ↗

Formate and potassium ions affect Escherichia coli proton ATPase activity at low pH during mixed carbon fermentation.Semantic proximity Read ↗

Redox sensing by Escherichia coli: effects of copper ions as oxidizers on proton-coupled membrane transport.Semantic proximity Read ↗

Dependence on the F0F1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases 1 and 2 during glucose and glycerol fermentation at high and low pH in Escherichia coli.Semantic proximity Read ↗

The roles of hydrogenases 3 and 4, and the F0F1-ATPase, in H2 production by Escherichia coli at alkaline and acidic pH.Semantic proximity Read ↗

Formate hydrogenlyase is needed for proton-potassium exchange through the F0F1-ATPase and the TrkA system in anaerobically grown and glycolysing Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.