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Systematic kinetics study of FoF1-ATPase: analytic results and comparison with experiments.

Authors
  • Shu, Yao-Gen
  • Lai, Pik-Yin
Type
Published Article
Journal
The Journal of Physical Chemistry B
Publisher
American Chemical Society
Publication Date
Oct 23, 2008
Volume
112
Issue
42
Pages
13453–13459
Identifiers
DOI: 10.1021/jp8052696
PMID: 18816087
Source
Medline
License
Unknown

Abstract

The systematic kinetics of the holoenzyme F oF 1-ATPase has been investigated by a tri-site filled, random binding order, and stochastic mechanochemical tight coupling model. The connection between the mechanical rotation speed and the chemical quantities such as the concentrations of substrates, the proton motive force, and the mechanical damping coefficient, has been analytically derived. The enzymatics based on ensemble experiments and single-molecule assays can be discussed systematically. Our model predictions agree well with both ensemble and single-molecule experimental results. Furthermore, this model can be used to study the dynamics of F oF 1-ATPase in a vesicle system.

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