Critical evaluation of the one- versus the two-channel model for the operation of the ATP synthase’s Fo motor
- 15 August 2000
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1459 (2-3) , 506-513
- https://doi.org/10.1016/s0005-2728(00)00190-0
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Crucial Role of the Membrane Potential for ATP Synthesis by F1Fo ATP SynthasesJournal of Experimental Biology, 2000
- Structure and Function of the Fo Complex of the ATP Synthase from Escherichia ColiJournal of Experimental Biology, 2000
- Energy transduction in the sodium F-ATPase of Propionigenium modestumProceedings of the National Academy of Sciences, 1999
- Interacting helical faces of subunits a and c in the F 1 F o ATP synthase of Escherichia coli defined by disulfide cross-linkingProceedings of the National Academy of Sciences, 1998
- Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP SynthaseBiochemistry, 1998
- ATP synthase: an electrochemical ransducer with rotatory mechanicsTrends in Biochemical Sciences, 1997
- The F0 Complex of the Escherichia Coli ATP SynthaseEuropean Journal of Biochemistry, 1995
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Formation of a functionally active sodium‐translocating hybrid F1F0 ATPase in Escherichia coli by homologous recombinationEuropean Journal of Biochemistry, 1993
- ATP formation caused by acid-base transition of spinach chloroplasts.Proceedings of the National Academy of Sciences, 1966