ROTATIONAL COUPLING IN THE F0F1 ATP SYNTHASE
- 1 June 1999
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics
- Vol. 28 (1) , 205-234
- https://doi.org/10.1146/annurev.biophys.28.1.205
Abstract
The F0F1 ATP synthase is a large multisubunit complex that couples translocation of protons down an electrochemical gradient to the synthesis of ATP. Recent advances in structural analyses have led to the demonstration that the enzyme utilizes a rotational catalytic mechanism. Kinetic and biochemical evidence is consistent with the expected equal participation of the three catalytic sites in the alpha 3 beta 3 hexamer, which operate in sequential, cooperative reaction pathways. The rotation of the core gamma subunit plays critical roles in establishing the conformation of the sites and the cooperative interactions. Mutational analyses have shown that the rotor subunits are responsible for coupling and in doing so transmit specific conformational information between transport and catalysis.Keywords
This publication has 133 references indexed in Scilit:
- Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP SynthaseBiochemistry, 1998
- Topographical structure of membrane‐bound Escherichia coli F1F0 ATP synthase in aqueous bufferFEBS Letters, 1996
- Molecular imaging of Escherichia coli F0F1‐ATPase in reconstituted membranes using atomic force microscopyFEBS Letters, 1996
- Differentiation of Catalytic Sites on Escherichia coli F1ATPase by Laser Photoactivated Labeling with [3H]-2-Azido-ATP Using the Mutant βGlu381Cys:εSer108Cys To Identify Different β Subunits by Their Interactions with γ and ε SubunitsBiochemistry, 1996
- The Human Integrin α8β1 Functions as a Receptor for Tenascin, Fibronectin, and VitronectinPublished by Elsevier ,1995
- Coupling between catalytic sites and the proton channel in F1F0-type ATPasesTrends in Biochemical Sciences, 1994
- Structure and Mechanism of F 0 F 1 ‐Type ATP Synthases and ATPasesPublished by Wiley ,1991
- The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimensFEBS Letters, 1987
- Mode of inhibition of sodium azide on H+‐ATPase of Escherichia coliFEBS Letters, 1987
- Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coliBiochemical and Biophysical Research Communications, 1977