2002/05/02 by Yaroslav Zolotaryuk, A. V. Zolotaryuk, V. N. Ermakov +8
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #ATP Synthase and ATPases Research #Advanced Thermodynamics and Statistical Mechanics #Biological Physics (physics.bio-ph) #FOS: Biological sciences #FOS: Physical sciences #Quantitative Biology (q-bio) #physics.bio-ph #q-bio
paper · pdf · doi:10.48550/arxiv.physics/0205005
7 figures
arxiv created 2002/05/02 · openalex publication_date 2002/05/02 · arxiv updated 2009/12/01 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/28
Two simple (rotator and one-particle) mechanistic models are suggested to describe simultaneously at a minimal level of sophistication two basic functions of F1-ATPase: a motor regime driven by ATP hydrolysis and its inverted function as ATP synthesis. This description is consistent with the so-called rotary binding-change mechanism, a milestone of functioning ATP synthase, and uses a stepping (driving) function associated with two sequences of time instants, at which hydrolysis and synthesis reactions occur. It is useful to analyse experimental data and numerical simulations indeed predict corresponding dynamic behavior.