Systematic kinetics study of FoF1-ATPase: analytic results and comparison with experiments.
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.
Shu
Yao-Gen
YG
Department of Physics, National Central University, Chung-Li, Taiwan 320, Republic of China. shuyg@itp.ac.cn
Lai
Pik-Yin
PY
D001696:Biomechanical Phenomena; D006867:Hydrolases / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D013269:Stochastic Processes
D006867:Hydrolases; D006180:Proton-Translocating ATPases