title: Chemomechanical coupling mechanism of F(1)-ATPase: catalysis and torque generation.
abstract: F1-ATPase (F1), a rotary motor protein driven by ATP hydrolysis, is unique with respect to its high efficiency and reversibility in converting chemical energy into mechanical work. Single-molecule studies have improved our understanding about the energy-conversion mechanism of F1 and the chemomechanical-coupling scheme under ATP hydrolysis conditions. A novel single-molecule technique was recently established to estimate the free-energy change of F1 during catalysis at elementary-step resolution, advancing our understanding about the energy-conversion mechanism of ATP hydrolysis and synthesis. The energy conversion mechanism of F1 elucidated from single-molecule studies provides us with important insights into the operating principles underlying molecular motors.
authors: Department of Applied Chemistry, School of Engineering, The University of Tokyo, Tokyo 113-8656, Japan.
authors: Rikiya
authors: R
authors: Watanabe
authors: Hiroyuki
authors: H
authors: Noji
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D055162:Biocatalysis; D006801:Humans; D006868:Hydrolysis; D008958:Models, Molecular; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics; D019415:Torque
chemical_list: D021122:Protein Subunits; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases