ArticleNature2014
Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
65 citing papers in PubMed, 134 citations in OpenAlex.
- A Bacillales-specific tubular scaffold essential for NADH dehydrogenase activity.Nature communications · 2026Article
- Conformational Dynamics of NaJournal of chemical information and modeling · 2026Article
- The redox driven NaNature communications · 2026Article
- Molecular Dynamics Analysis of Inhibitor Binding Interactions in the Vibrio cholerae Respiratory Complex NQR.Proteins · 2026Article
- Synthesis, Biological Evaluation, and Computational Analysis of 1,4-Naphthoquinone Derivatives as Inhibitors of the Sodium-Dependent NADH:Ubiquinone Oxidoreductase (NQR) inInternational journal of molecular sciences · 2026Article
- Integrating natural language processing and genome analysis enables accurate bacterial phenotype prediction.NAR genomics and bioinformatics · 2025Article
- Machine learning-guided in Silico identification of Na⁺-NQR inhibitors from Berberis vulgaris and Hydrastis Canadensis phytochemicals against Vibrio cholerae.Scientific reports · 2025Article
- The RNF/NQR redox pumps: a versatile system for energy transduction in bacteria and archaea.Applied microbiology and biotechnology · 2025Review
- Structural Elucidation of the Mechanism for Inhibitor Resistance in the NaBiochemistry · 2025Article
- Molecular principles of redox-coupled sodium pumping of the ancient Rnf machinery.Nature communications · 2025Article
- NQR as a target for new antibiotics.Frontiers in microbiology · 2025Review
- Essential genes formSystems · 2024Article
- Versatile roles of protein flavinylation in bacterial extracyotosolic electron transfer.mSystems · 2024Article
- Architecture of the RNF1 complex that drives biological nitrogen fixation.Nature chemical biology · 2024Article
- Functionality of the NaArchives of microbiology · 2023Article
- Conformational coupling of redox-driven NaNature structural & molecular biology · 2023Article
- Characterization of two bacterial multi-flavinylated proteins harboring multiple covalent flavin cofactors.BBA advances · 2023Article
- Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Purification and structural characterization of the NaNature communications · 2022Article
- Cryo-EM structures of NaNature communications · 2022Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NADH oxidation in the respiratory chain is coupled to ion translocation across the membrane to build up an electrochemical gradient. The sodium-translocating NADH:quinone oxidoreductase (Na(+)-NQR), a membrane protein complex widespread among pathogenic bacteria, consists of six subunits, NqrA, B, C, D, E and F. To our knowledge, no structural information on the Na(+)-NQR complex has been available until now. Here we present the crystal structure of the Na(+)-NQR complex at 3.5 Å resolution. The arrangement of cofactors both at the cytoplasmic and the periplasmic side of the complex, together with a hitherto unknown iron centre in the midst of the membrane-embedded part, reveals an electron transfer pathway from the NADH-oxidizing cytoplasmic NqrF subunit across the membrane to the periplasmic NqrC, and back to the quinone reduction site on NqrA located in the cytoplasm. A sodium channel was localized in subunit NqrB, which represents the largest membrane subunit of the Na(+)-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na(+) translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na(+) through the observed channel.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.