The Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I) Is a Primary Proton Pump but May Be Capable of Secondary Sodium Antiport
Open Access
- 1 April 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (18) , 18377-18383
- https://doi.org/10.1074/jbc.m311242200
Abstract
No abstract availableKeywords
This publication has 57 references indexed in Scilit:
- The nuclear encoded subunits of complex I from bovine heart mitochondriaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2003
- Modular Evolution of the Respiratory NADH:Ubiquinone Oxidoreductase and the Origin of its ModulesJournal of Theoretical Biology, 1997
- Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conductionBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1997
- H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cellsJournal of Bacteriology, 1996
- The proton‐pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplastsFEBS Letters, 1995
- The NADH:ubiquinone oxidoreductase (complex I) of respiratory chainsQuarterly Reviews of Biophysics, 1992
- The respiratory‐chain NADH dehydrogenase (complex I) of mitochondriaEuropean Journal of Biochemistry, 1991
- Mechanistic stoichiometry of mitochondrial oxidative phosphorylationBiochemistry, 1991
- Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratioBiochemical Journal, 1988
- Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinoneFEBS Letters, 1984