Monte Carlo simulation from proton slip to “coupled” proton flow in ATP synthase based on the bi-site mechanism-Reference-Cited by-同舟云学术

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Monte Carlo simulation from proton slip to “coupled” proton flow in ATP synthase based on the bi-site mechanism

Published:2011-09 Issue:3 Volume:105 Page:233-237
ISSN:0303-2647
Container-title:Biosystems
language:en
Short-container-title:Biosystems

Author:

Qian Jun,Liang Jian

Publisher

Elsevier BV

Subject

Applied Mathematics,General Biochemistry, Genetics and Molecular Biology,Modelling and Simulation,General Medicine,Statistics and Probability

Reference40 articles.

1. Structure at 2.8 resolution of F1-ATPase from bovine heart mitochondria;Abrahams;Nature,1994

2. Coupling of rotation and catalysis in F-1-ATPase revealed by single-molecule imaging and manipulation;Adachi;Cell,2007

3. The Escherichia coli FoF1 γM23K uncoupling mutant has a higher K0.5 for Pi transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway;Al-Shawi;Biochemistry,1997

4. Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy;Bernal;Structure,2004

5. Catalytic site occupancy during ATP synthase catalysis;Boyer;FEBS Letters,2002

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Combined mathematical methods in the description of the FoF1-ATP synthase catalytic cycle;Mathematical Biosciences;2013-05

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