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

Yao Gen Shu, Pik Yin Lai

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)13453-13459
Number of pages7
JournalJournal of Physical Chemistry B
Volume112
Issue number42
DOIs
StatePublished - 23 Oct 2008

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