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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Highly coupled ATP synthesis by F1-ATPase single molecules
Yannick Rondelez1, Guillaume Tresset, Takako Nakashima
1LIMMS/CNRS-IIS, Tokyo 153-8505, Japan.
Nature
|February 18, 2005
Summary
The F1-ATPase motor
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- F1-ATPase is a rotary motor essential for ATP synthesis.
- Its function in the F0F1 complex involves driven clockwise rotation for ATP production.
- Understanding the efficiency of this mechanochemical transformation is crucial.
Purpose of the Study:
- To measure the yield of the mechanochemical transformation in F1-ATPase.
- To investigate the role of the epsilon-subunit in ATP synthesis efficiency.
- To provide direct evidence of catalytic reaction and mechanical rotation coupling.
Main Methods:
- Utilized single-molecule manipulation and microfabrication techniques.
- Enclosed single F1 molecules in femtolitre-sized hermetic chambers.
- Employed magnetic tweezers to induce controlled rotation and measured subsequent anticlockwise rotation.
Main Results:
- Mechanochemical coupling efficiency was low for F1-ATPase without the epsilon-subunit.
- Efficiency reached up to 77% for F1-ATPase reconstituted with the epsilon-subunit (F1+epsilon).
- Synthesized ATP amount correlated with anticlockwise rotation speed.
Conclusions:
- F1-ATPase is designed for tight coupling between catalytic reactions and mechanical rotation.
- The epsilon-subunit plays an essential role in efficient ATP synthesis.
- This study provides direct evidence for the functional significance of the epsilon-subunit in the F0F1 motor.
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