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Chemomechanical coupling mechanism of F 1 ‐ATPase: Catalysis and torque generation
Author(s) -
Watanabe Rikiya,
Noji Hiroyuki
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.01.063
Subject(s) - atp hydrolysis , atpase , molecular motor , chemistry , mechanism (biology) , energy transformation , hydrolysis , work (physics) , coupling (piping) , chemical energy , torque , catalysis , molecule , chemical physics , mechanical energy , biophysics , combinatorial chemistry , nanotechnology , enzyme , materials science , thermodynamics , biochemistry , physics , organic chemistry , power (physics) , biology , quantum mechanics , metallurgy
F 1 ‐ATPase ( F 1 ), 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 F 1 and the chemomechanical‐coupling scheme under ATP hydrolysis conditions. A novel single‐molecule technique was recently established to estimate the free‐energy change of F 1 during catalysis at elementary‐step resolution, advancing our understanding about the energy‐conversion mechanism of ATP hydrolysis and synthesis. The energy conversion mechanism of F 1 elucidated from single‐molecule studies provides us with important insights into the operating principles underlying molecular motors.