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

Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli.

Biochimica et biophysica acta - 30 Sept 2005

Zuber D, Krause R, Venturi M, Padan E, Bamberg E, Fendler K

Abstract excerpt

The Na+/H+ antiporter NhaA is the main Na+ extrusion system in E. coli. Using direct current measurements combined with a solid supported membrane (SSM), we obtained electrical data of the function of NhaA purified and reconstituted in liposomes. These measurements demonstrate NhaA's electrogenicity, its specificity for Li+ and Na+ and its pronounced pH dependence in the range pH 6.5-8.5. The mutant G338S, in...

Read the complete abstract on PubMed

Topics

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

Share to Biological Transport, Active
Share to Electrophysiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Ion Transport

Share to Liposomes

Share to Sodium

Share to Sodium-Hydrogen Exchangers

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 16139785
DOI: 10.1016/j.bbabio.2005.07.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli.PMID 16139785Read ↗

Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.Semantic proximity Read ↗

Lysine 300 is essential for stability but not for electrogenic transport of the Escherichia coli NhaA Na+/H+ antiporter.Semantic proximity Read ↗

Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli.Semantic proximity Read ↗

NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential.Semantic proximity Read ↗

Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.Semantic proximity Read ↗

Helix VIII of NhaA Na(+)/H(+) antiporter participates in the periplasmic cation passage and pH regulation of the antiporter.Semantic proximity Read ↗

A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli.Semantic proximity Read ↗

NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter.Semantic proximity Read ↗

Regulation of NhaA by protons.Semantic proximity Read ↗

Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli.Semantic proximity Read ↗

Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters.Semantic proximity Read ↗

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.Semantic proximity Read ↗

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