F1-ATPase can Rotate in the Correct Direction, without its Rotary Shaft
نویسندگان
چکیده
منابع مشابه
F1-ATPase: a highly coupled reversible rotary motor.
F1 (F1-ATPase) is a highly coupled rotary molecular motor and hydrolyses three ATP molecules per turn (3 ATP/turn). Recently, we have developed femtolitre reaction chamber arrays for highly sensitive measurement of biological reactions. By combining this technique with the rotating magnetic tweezers, the coupling ratio of the reverse reaction, ATP synthesis catalysed by single F1 molecules, has...
متن کاملF1-ATPase: A Rotary Motor Made of a Single Molecule
synthesis/hydrolysis of ATP in F 1 ? Almost 20 years ago Paul Boyer made a radical proposal that the two reactions are mechanically coupled by rotation of a common shaft penetrating F 0 and F 1 (see Boyer, 1997). Part of his * Department of Physics reasoning was that F1 contains three catalytic sites, one Faculty of Science and Technology on each , which participate on average equally in ATP K...
متن کاملF1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft
F1F0 ATP synthase (ATPase) either facilitates the synthesis of ATP in a process driven by the proton moving force (pmf), or uses the energy from ATP hydrolysis to pump protons against the concentration gradient across the membrane. ATPase is composed of two rotary motors, F0 and F1, which compete for control of their shared γ -shaft. We present a self-consistent physical model of F1 motor as a ...
متن کاملNovel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.
The crystal structure of yeast mitochondrial F(1) ATPase contains three independent copies of the complex, two of which have similar conformations while the third differs in the position of the central stalk relative to the alpha(3)beta(3) sub-assembly. All three copies display very similar asymmetric features to those observed for the bovine enzyme, but the yeast F(1) ATPase structures provide...
متن کاملMechanochemical Energy Transduction during the Main Rotary Step in the Synthesis Cycle of F1-ATPase.
F1-ATPase is a highly efficient molecular motor that can synthesize ATP driven by a mechanical torque. Its ability to function reversibly in either direction requires tight mechanochemical coupling between the catalytic domain and the rotating central shaft, as well as temporal control of substrate binding and product release. Despite great efforts and significant progress, the molecular detail...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2010
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.50.120