Literature DB >> 22465856

Insights into the mechanism of electron transfer and sodium translocation of the Na(+)-pumping NADH:quinone oxidoreductase.

Oscar Juárez1, Blanca Barquera.   

Abstract

Na(+)-NQR is a unique energy-transducing complex, widely distributed among marine and pathogenic bacteria. It converts the energy from the oxidation of NADH and the reduction of quinone into an electrochemical Na(+)-gradient that can provide energy for the cell. Na(+)-NQR is not homologous to any other respiratory protein but is closely related to the RNF complex. In this review we propose that sodium pumping in Na(+)-NQR is coupled to the redox reactions by a novel mechanism, which operates at multiple sites, is indirect and mediated by conformational changes of the protein. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).
Copyright © 2012 Elsevier B.V. All rights reserved.

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Year:  2012        PMID: 22465856     DOI: 10.1016/j.bbabio.2012.03.017

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  29 in total

1.  The Kinetic Reaction Mechanism of the Vibrio cholerae Sodium-dependent NADH Dehydrogenase.

Authors:  Karina Tuz; Katherine G Mezic; Tianhao Xu; Blanca Barquera; Oscar Juárez
Journal:  J Biol Chem       Date:  2015-05-23       Impact factor: 5.157

Review 2.  The sodium pumping NADH:quinone oxidoreductase (Na⁺-NQR), a unique redox-driven ion pump.

Authors:  Blanca Barquera
Journal:  J Bioenerg Biomembr       Date:  2014-07-23       Impact factor: 2.945

3.  Characterization of the Pseudomonas aeruginosa NQR complex, a bacterial proton pump with roles in autopoisoning resistance.

Authors:  Daniel A Raba; Monica Rosas-Lemus; William M Menzer; Chen Li; Xuan Fang; Pingdong Liang; Karina Tuz; David D L Minh; Oscar Juárez
Journal:  J Biol Chem       Date:  2018-08-22       Impact factor: 5.157

4.  Dynamic energy dependency of Chlamydia trachomatis on host cell metabolism during intracellular growth: Role of sodium-based energetics in chlamydial ATP generation.

Authors:  Pingdong Liang; Mónica Rosas-Lemus; Dhwani Patel; Xuan Fang; Karina Tuz; Oscar Juárez
Journal:  J Biol Chem       Date:  2017-11-09       Impact factor: 5.157

5.  Identification of the binding sites for ubiquinone and inhibitors in the Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae by photoaffinity labeling.

Authors:  Takeshi Ito; Masatoshi Murai; Satoshi Ninokura; Yuki Kitazumi; Katherine G Mezic; Brady F Cress; Mattheos A G Koffas; Joel E Morgan; Blanca Barquera; Hideto Miyoshi
Journal:  J Biol Chem       Date:  2017-03-15       Impact factor: 5.157

6.  The Staphylococcus aureus NuoL-like protein MpsA contributes to the generation of membrane potential.

Authors:  Sonja Mayer; Wojtek Steffen; Julia Steuber; Friedrich Götz
Journal:  J Bacteriol       Date:  2014-12-01       Impact factor: 3.490

7.  Comprehensive Genomic Analyses of the OM43 Clade, Including a Novel Species from the Red Sea, Indicate Ecotype Differentiation among Marine Methylotrophs.

Authors:  Francy Jimenez-Infante; David Kamanda Ngugi; Manikandan Vinu; Intikhab Alam; Allan Anthony Kamau; Jochen Blom; Vladimir B Bajic; Ulrich Stingl
Journal:  Appl Environ Microbiol       Date:  2015-12-11       Impact factor: 4.792

8.  Inhibitors of a Na+-pumping NADH-ubiquinone oxidoreductase play multiple roles to block enzyme function.

Authors:  Takahiro Masuya; Yuki Sano; Hinako Tanaka; Nicole L Butler; Takeshi Ito; Tatsuhiko Tosaki; Joel E Morgan; Masatoshi Murai; Blanca Barquera; Hideto Miyoshi
Journal:  J Biol Chem       Date:  2020-07-20       Impact factor: 5.157

9.  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.

Authors:  Madeleine Strickland; Oscar Juárez; Yashvin Neehaul; Darcie A Cook; Blanca Barquera; Petra Hellwig
Journal:  J Biol Chem       Date:  2014-07-08       Impact factor: 5.157

10.  Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.

Authors:  Yulia V Bertsova; Maria S Fadeeva; Vitaly A Kostyrko; Marina V Serebryakova; Alexander A Baykov; Alexander V Bogachev
Journal:  J Biol Chem       Date:  2013-04-04       Impact factor: 5.157

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