ArticleThe Journal of biological chemistry2015
The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Quinolone inhibitors targetingEuropean journal of medicinal chemistry reports · 2026Article
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- 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
- Structural Elucidation of the Mechanism for Inhibitor Resistance in the NaBiochemistry · 2025Article
- NQR as a target for new antibiotics.Frontiers in microbiology · 2025Review
- The respiratory chain ofFrontiers in microbiology · 2024Article
- Sodium/(calcium + potassium) exchanger NCKX4 optimizes KLK4 activity in the enamel matrix microenvironment to regulate ECM modeling.Frontiers in physiology · 2023Article
- Cryo-EM structures of NaNature communications · 2022Article
- The side chain of ubiquinone plays a critical role in NaBiochimica et biophysica acta. Bioenergetics · 2022Article
- Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB inMedComm · 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
- Structural and ligand binding analyses of the periplasmic sensor domain of RsbU in Chlamydia trachomatis support a role in TCA cycle regulation.Molecular microbiology · 2020Article
- The aerobic respiratory chain of Pseudomonas aeruginosa cultured in artificial urine media: Role of NQR and terminal oxidases.PloS one · 2020Article
- Role of Subunit D in Ubiquinone-Binding Site ofACS omega · 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sodium-dependent NADH dehydrogenase (Na(+)-NQR) is the main ion transporter in Vibrio cholerae. Its activity is linked to the operation of the respiratory chain and is essential for the development of the pathogenic phenotype. Previous studies have described different aspects of the enzyme, including the electron transfer pathways, sodium pumping structures, cofactor and subunit composition, among others. However, the mechanism of the enzyme remains to be completely elucidated. In this work, we have studied the kinetic mechanism of Na(+)-NQR with the use of steady state kinetics and stopped flow analysis. Na(+)-NQR follows a hexa-uni ping-pong mechanism, in which NADH acts as the first substrate, reacts with the enzyme, and the oxidized NAD leaves the catalytic site. In this conformation, the enzyme is able to capture two sodium ions and transport them to the external side of the membrane. In the last step, ubiquinone is bound and reduced, and ubiquinol is released. Our data also demonstrate that the catalytic cycle involves two redox states, the three- and five-electron reduced forms. A model that gathers all available information is proposed to explain the kinetic mechanism of Na(+)-NQR. This model provides a background to understand the current structural and functional information.
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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.