Systematic kinetics study of F0F1-ATPase: Analytic results and comparison with experiments

Yao Gen Shu, Pik Yin Lai

研究成果: 雜誌貢獻期刊論文同行評審

13 引文 斯高帕斯(Scopus)

摘要

The systematic kinetics of the holoenzyme F0F1-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 F0F 1-ATPase in a vesicle system.

原文???core.languages.en_GB???
頁(從 - 到)13453-13459
頁數7
期刊Journal of Physical Chemistry B
112
發行號42
DOIs
出版狀態已出版 - 23 10月 2008

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