Abstract
F1-ATPase, a water-soluble portion of ATP synthase, is a fully reversible rotary molecular machine in which a central γ subunit rotates inside a cylinder made of three α and three β subunits alternately arranged. This motor rotates counterclockwise by hydrolyzing ATP in three catalytic sites but synthesizes ATP when forced to rotate clockwise by an external force. Single-molecule studies have revealed how the chemical reactions that occur in the three catalytic sites are coupled to mechanical rotation.
| Original language | English |
|---|---|
| Title of host publication | Comprehensive Biophysics |
| Publisher | Elsevier Inc. |
| Pages | 35-49 |
| Number of pages | 15 |
| Volume | 8 |
| ISBN (Print) | 9780080957180 |
| DOIs | |
| Publication status | Published - 2012 |
| Externally published | Yes |
Keywords
- ATP synthase
- Chemo-mechanical coupling
- Conformational change
- F-ATPase
- Fluorescent ATP analog
- Free energy
- High efficiency
- High-speed imaging
- Induced fit
- Molecular motor
- Power stroke
- Single fluorophore imaging
- Single-molecule study
- Torque generation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)