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

Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I).

The Journal of biological chemistry - 19 Sept 2008

Nakamaru-Ogiso Eiko, Matsuno-Yagi Akemi, Yoshikawa Shinya, Yagi Takao, Ohnishi Tomoko

Abstract excerpt

NADH:quinone oxidoreductase (complex I) plays a central role in cellular energy metabolism, and its dysfunction is found in numerous human mitochondrial diseases. Although the understanding of its structure and function has been limited, the x-ray crystal structure of the hydrophilic part of Thermus thermophilus complex I recently became available. It revealed the localization of all redox centers, including 9...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Electron Spin Resonance Spectroscopy

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

Share to Electron Transport Complex I

Share to Iron-Sulfur Proteins

Share to Ligands

Share to NADH Dehydrogenase

Share to Oligonucleotides

Share to Oxidation-Reduction

Source

Open in PubMed Open full text

Identifiers

PMID: 18603533
DOI: 10.1074/jbc.M804015200
PMCID: PMC2533800

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

Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I).PMID 18603533Read ↗

Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.Semantic proximity Read ↗

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

Structure of the peripheral arm of a minimalistic respiratory complex I.Semantic proximity Read ↗

Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB.Semantic proximity Read ↗

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

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

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

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

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

Structural robustness of the NADH binding site in NADH:ubiquinone oxidoreductase (complex I).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.