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Multiscale Sampling of a Heterogeneous Water/Metal Catalyst Interface using Density Functional Theory and Force-Field Molecular Dynamics
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Catalytic dwell oscillations complete the F1-ATPase mechanism
Zain A Bukhari1, Wayne D Frasch2
1School of Life Sciences, Arizona State University, Tempe, AZ, USA.
Communications Chemistry
|February 21, 2025
Summary
The F1-ATPase motor
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- F1-ATPase is a rotary molecular motor essential for cellular energy production.
- Its mechanism involves the rotation of the gamma subunit within a ring of catalytic sites.
- Previous models did not fully explain observed structural states during ATP hydrolysis.
Purpose of the Study:
- To investigate the catalytic dwell states of the F1-ATPase motor.
- To elucidate the role of subunit-gamma oscillations in the rotary mechanism.
- To reconcile newly observed states with the canonical F1-ATPase mechanism.
Main Methods:
- High-resolution time-resolved monitoring of subunit-gamma rotary position in E. coli F1-ATPase.
- Analysis of oscillation patterns during catalytic dwells.
- Correlation of observed states with structural data and ATP hydrolysis.
Main Results:
- Stage-1 catalytic dwells show oscillations centered at 0°, consistent with ATP hydrolysis.
- Stage-2 oscillations exhibit distinct populations centered at 14° and 33°, related to ATP binding.
- Stage-3 involves subunit-gamma returning to 0°, ensuring phased power strokes.
Conclusions:
- Catalytic dwell oscillations persist until correct substrate and product occupancy is achieved.
- These oscillations are crucial for maintaining the synchrony of consecutive power strokes.
- The findings complete the understanding of the F1-ATPase rotary mechanism.
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