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Method to extract multiple states in F1-ATPase rotation experiments from jump distributions.

Sándor Volkán-Kacsó1,2, Luan Q Le3, Kaicheng Zhu4

  • 1Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125; ram@caltech.edu svk@caltech.edu haibinsu@ust.hk.

Proceedings of the National Academy of Sciences of the United States of America
|November 29, 2019
PubMed
Summary

This study introduces a new method to analyze fast single-molecule rotation in F1-adenosinetriphosphatase (F1-ATPase) by examining angular jump distributions. The findings reveal transient states, offering new insights into enzyme mechanisms.

Keywords:
4-state modelADP releaseF-ATPaseconcerted dynamicssingle-molecule imaging

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Area of Science:

  • Biophysics
  • Enzyme kinetics
  • Single-molecule biophysics

Background:

  • F1-adenosinetriphosphatase (F1-ATPase) is a molecular motor crucial for cellular energy production.
  • Understanding the rapid dynamics of F1-ATPase is essential for elucidating its catalytic mechanism.
  • Existing methods like the "stalling" technique provide valuable but incomplete insights into F1-ATPase function.

Purpose of the Study:

  • To develop and validate a novel method for analyzing fast single-molecule rotation trajectories in F1-ATPase.
  • To identify transient states and conformational changes not readily detectable by other techniques.
  • To complement existing methods and provide a more comprehensive understanding of F1-ATPase's catalytic cycle.

Main Methods:

  • Analysis of fast (10 μs) single-molecule rotation trajectories.
  • Utilizing the distribution of angular jumps during transitions between catalytic dwells.
  • Application of multistate theory incorporating viscoelastic fluctuations of the imaging probe.

Main Results:

  • A bimodal distribution of angular jumps was observed, indicating the presence of multiple states at the same rotation angle.
  • A theoretical profile of angular jumps was predicted using a 3-state model, showing good agreement with experimental data.
  • Inclusion of a fourth transient state (∼10 μs lifetime) improved agreement, suggesting a rapid ATP binding and ADP release transient.

Conclusions:

  • The proposed method effectively reveals transient states in F1-ATPase, complementing existing techniques.
  • A transient state with a lifetime of approximately 10 μs was identified, significantly shorter than previously characterized ADP release events.
  • The findings provide a more detailed mechanistic understanding of the F1-ATPase catalytic cycle, particularly the interplay of ATP binding and ADP release.