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

Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.

Journal of biochemistry - 1 Oct 2016

Narayanan Madhavan, Sakyiama Joseph A, Elguindy Mahmoud M, Nakamaru-Ogiso Eiko

Abstract excerpt

Respiratory complex I has an L-shaped structure formed by the hydrophilic arm responsible for electron transfer and the membrane arm that contains protons pumping machinery. Here, to gain mechanistic insights into the role of subunit NuoL, we investigated the effects of Mg2+, Zn2+ and the Na+/H+ antiporter inhibitor 5-(N-ethyl-N-isopropyl)-amiloride (EIPA) on proton pumping activities of various isolated NuoL...

Read the complete abstract on PubMed

Topics

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

Share to Amiloride
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex I

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Mutation

Share to NADH Dehydrogenase

Source

Open in PubMed Open full text

Identifiers

PMID: 27118783
DOI: 10.1093/jb/mvw027
PMCID: PMC5048018

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

Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.PMID 27118783Read ↗

The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.Semantic proximity Read ↗

Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.Semantic proximity Read ↗

Critical roles of subunit NuoH (ND1) in the assembly of peripheral subunits with the membrane domain of Escherichia coli NDH-1.Semantic proximity Read ↗

Roles of subunit NuoK (ND4L) in the energy-transducing mechanism of Escherichia coli NDH-1 (NADH:quinone oxidoreductase).Semantic proximity Read ↗

A universal coupling mechanism of respiratory complex I.Semantic proximity Read ↗

Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).Semantic proximity Read ↗

Features of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.Semantic proximity Read ↗

Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).Semantic proximity Read ↗

Involvement of Acidic Amino Acid Residues in Zn(2+) Binding to Respiratory Complex I.Semantic proximity Read ↗

Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.Semantic proximity Read ↗

Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.Semantic proximity Read ↗

Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli.Semantic proximity Read ↗

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