title: Monte Carlo simulation from proton slip to "coupled" proton flow in ATP synthase based on the bi-site mechanism.
abstract: ATP synthase couples proton flow to ATP synthesis, but is leaky to protons at very low nucleotide concentration. Based on the bi-site mechanism, we simulated the proton conduction from proton slip to "coupled" proton flow in ATP synthase using the Monte Carlo method. Good agreement is obtained between the simulated and available experimental results. Our model provides deeper insight into the nucleotide dependence of ATP catalysis, and the kinetic cooperativity in three catalysis subunits. The results of simulation support the bi-site mechanism in ATP synthesis.
authors.affiliation: School of Physics, Nankai University, No. 94 Weijing Road, Nankai District, Tianjin, China. qianjun@nankai.edu.cn
authors.forename: Jun
authors.initials: J
authors.lastname: Qian
authors.forename: Jian
authors.initials: J
authors.lastname: Liang
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D002384:Catalysis; D020134:Catalytic Domain; D003198:Computer Simulation; D004789:Enzyme Activation; D007700:Kinetics; D008954:Models, Biological; D009010:Monte Carlo Method; D009711:Nucleotides / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons
chemical_list: D009711:Nucleotides; D011522:Protons; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases