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Acceleration of the ATP‐binding rate of F 1 ‐ATPase by forcible forward rotation
Author(s) -
Iko Yuko,
Tabata Kazuhito V.,
Sakakihara Shouichi,
Nakashima Takako,
Noji Hiroyuki
Publication year - 2009
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.2009.08.042
Subject(s) - atp hydrolysis , atpase , rotation (mathematics) , chemistry , biophysics , f atpase , atp synthase , reaction rate constant , coupling (piping) , rotor (electric) , catalysis , hydrolysis , adenosine triphosphate , rotary engine , acceleration , crystallography , physics , kinetics , enzyme , biochemistry , materials science , biology , classical mechanics , geometry , mathematics , thylakoid , chloroplast , quantum mechanics , gene , metallurgy , composite material
F 1 ‐ATPase (F 1 ) is a reversible ATP‐driven rotary motor protein. When its rotary shaft is reversely rotated, F 1 produces ATP against the chemical potential of ATP hydrolysis, suggesting that F 1 modulates the rate constants and equilibriums of catalytic reaction steps depending on the rotary angle of the shaft. Although the chemomechanical coupling scheme of F 1 has been determined, it is unclear how individual catalytic reaction steps depend on its rotary angle. Here, we report direct evidence that the ATP‐binding rate of F 1 increases upon the forward rotation of the rotor, and its binding affinity to ATP is enhanced by rotation.