ArticleThe Journal of biological chemistry2012
The role of glycine residues 140 and 141 of subunit B in the functional ubiquinone binding site of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Molecular Dynamics Analysis of Inhibitor Binding Interactions in the Vibrio cholerae Respiratory Complex NQR.Proteins · 2026Article
- Structural Elucidation of the Mechanism for Inhibitor Resistance in the NaBiochemistry · 2025Article
- NQR as a target for new antibiotics.Frontiers in microbiology · 2025Review
- Cryo-EM structures of NaNature communications · 2022Article
- The side chain of ubiquinone plays a critical role in NaBiochimica et biophysica acta. Bioenergetics · 2022Article
- Molecular dynamics modeling of the Vibrio cholera NaMolecular and cellular biochemistry · 2022Article
- Article
- Specific chemical modification explores dynamic structure of the NqrB subunit in NaBiochimica et biophysica acta. Bioenergetics · 2021Article
- Inhibitors of a NaThe Journal of biological chemistry · 2020Article
- Role of Subunit D in Ubiquinone-Binding Site ofACS omega · 2019Article
- Antibiotic Korormicin A Kills Bacteria by Producing Reactive Oxygen Species.Journal of bacteriology · 2019Article
- Characterization of theThe Journal of biological chemistry · 2018Article
- Dynamic energy dependency ofThe Journal of biological chemistry · 2018Article
- Identification of the binding sites for ubiquinone and inhibitors in the NaThe Journal of biological chemistry · 2017Article
- Identification of the Catalytic Ubiquinone-binding Site ofThe Journal of biological chemistry · 2017Article
- The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase.The Journal of biological chemistry · 2015Article
- The conformational changes induced by ubiquinone binding in the Na+-pumping NADH:ubiquinone oxidoreductase (Na+-NQR) are kinetically controlled by conserved glycines 140 and 141 of the NqrB subunit.The Journal of biological chemistry · 2014Article
- The sodium pumping NADH:quinone oxidoreductase (Na⁺-NQR), a unique redox-driven ion pump.Journal of bioenergetics and biomembranes · 2014Review
- Article
- NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.The Journal of biological chemistry · 2013Article
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Na(+)-pumping NADH:quinone oxidoreductase (Na(+)-NQR) is the main entrance for electrons into the respiratory chain of many marine and pathogenic bacteria. The enzyme accepts electrons from NADH and donates them to ubiquinone, and the free energy released by this redox reaction is used to create an electrochemical gradient of sodium across the cell membrane. Here we report the role of glycine 140 and glycine 141 of the NqrB subunit in the functional binding of ubiquinone. Mutations at these residues altered the affinity of the enzyme for ubiquinol. Moreover, mutations in residue NqrB-G140 almost completely abolished the electron transfer to ubiquinone. Thus, NqrB-G140 and -G141 are critical for the binding and reaction of Na(+)-NQR with its electron acceptor, ubiquinone.
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