Energy transduction in the sodium F-ATPase of Propionigenium modestum
Open Access
- 27 April 1999
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 96 (9), 4924-4929
- https://doi.org/10.1073/pnas.96.9.4924
Abstract
The F-ATPase of the bacterium Propionigenium modestum is driven by an electrochemical sodium gradient between the cell interior and its environment. Here we present a mechanochemical model for the transduction of transmembrane sodium-motive force into rotary torque. The same mechanism is likely to operate in other F-ATPases, including the proton-driven F-ATPases of Escherichia coli.Keywords
This publication has 40 references indexed in Scilit:
- Arrangement of the Multicopy H+-translocating Subunit c in the Membrane Sector of the Escherichia coliF1F0 ATP SynthasePublished by Elsevier BV ,1998
- Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP SynthaseBiochemistry, 1998
- Membrane Topology of Subunit a of the F1F0 ATP Synthase as Determined by Labeling of Unique Cysteine ResiduesPublished by Elsevier BV ,1998
- Molecular Basis for the Coupling Ion Selectivity of F1F0 ATP Synthases: Probing the Liganding Groups for Na+ and Li+ in the c Subunit of the ATP Synthase from Propionigenium modestumBiochemistry, 1997
- Cross-linking of Engineered Subunit δ to (αβ)3 in Chloroplast F-ATPaseJournal of Biological Chemistry, 1996
- Topographical structure of membrane‐bound Escherichia coli F1F0 ATP synthase in aqueous bufferFEBS Letters, 1996
- THE F0F1-TYPE ATP SYNTHASES OF BACTERIA: Structure and Function of the F0 ComplexAnnual Review of Microbiology, 1996
- Molecular imaging of Escherichia coli F0F1‐ATPase in reconstituted membranes using atomic force microscopyFEBS Letters, 1996
- Transmembrane topology of Escherichia coli H+‐ATPase (ATP synthase) subunit aFEBS Letters, 1996
- A Double Mutation in Subunit c of the Na+-specific F1F0-ATPase ofPropionigenium modestumResults in a Switch from Na+to H+-coupled ATP Synthesis in theEscherichia coliHost CellsJournal of Molecular Biology, 1995