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

Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.

The Journal of biological chemistry - 21 Aug 2015

Zhu Shaotong, Vik Steven B

Abstract excerpt

Complex I (NADH:ubiquinone oxidoreductase) is a multisubunit, membrane-bound enzyme of the respiratory chain. The energy from NADH oxidation in the peripheral region of the enzyme is used to drive proton translocation across the membrane. One of the integral membrane subunits, nuoL in Escherichia coli, has an unusual lateral helix of ∼75 residues that lies parallel to the membrane surface and has been proposed to...

Read the complete abstract on PubMed

Topics

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

Share to Copper
Share to Cross-Linking Reagents
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex I

Share to NADH Dehydrogenase

Share to Periplasm

Share to Protons

Source

Open in PubMed Open full text

Identifiers

PMID: 26134569
DOI: 10.1074/jbc.M115.660381
PMCID: PMC4543639

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

Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.PMID 26134569Read ↗

Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Semantic proximity Read ↗

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

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

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

Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I.Semantic proximity Read ↗

A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli.Semantic proximity Read ↗

Human clinical mutations in mitochondrially encoded subunits of Complex I can be successfully modeled in E. coli.Semantic proximity Read ↗

Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).Semantic proximity Read ↗

Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex.Semantic proximity Read ↗

A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.Semantic proximity Read ↗

A Carboxylate Switch Point Controls Long-Range Energy Transduction in Respiratory Complex ISemantic proximity Read ↗

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