ArticleThe Journal of biological chemistry2014
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.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Cryo-EM structures of NaNature communications · 2022Article
- The side chain of ubiquinone plays a critical role in NaBiochimica et biophysica acta. Bioenergetics · 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
- 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 Na+-Translocating NADH:Quinone Oxidoreductase Enhances Oxidative Stress in the Cytoplasm of Vibrio cholerae.Journal of bacteriology · 2016Article
- The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Na(+)-pumping NADH:ubiquinone oxidoreductase (Na(+)-NQR) is responsible for maintaining a sodium gradient across the inner bacterial membrane. This respiratory enzyme, which couples sodium pumping to the electron transfer between NADH and ubiquinone, is not present in eukaryotes and as such could be a target for antibiotics. In this paper it is shown that the site of ubiquinone reduction is conformationally coupled to the NqrB subunit, which also hosts the final cofactor in the electron transport chain, riboflavin. Previous work showed that mutations in conserved NqrB glycine residues 140 and 141 affect ubiquinone reduction and the proper functioning of the sodium pump. Surprisingly, these mutants did not affect the dissociation constant of ubiquinone or its analog HQNO (2-n-heptyl-4-hydroxyquinoline N-oxide) from Na(+)-NQR, which indicates that these residues do not participate directly in the ubiquinone binding site but probably control its accessibility. Indeed, redox-induced difference spectroscopy showed that these mutations prevented the conformational change involved in ubiquinone binding but did not modify the signals corresponding to bound ubiquinone. Moreover, data are presented that demonstrate the NqrA subunit is able to bind ubiquinone but with a low non-catalytically relevant affinity. It is also suggested that Na(+)-NQR contains a single catalytic ubiquinone binding site and a second site that can bind ubiquinone but is not active.
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