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 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 کاملHigh-speed atomic force microscopy of protein dynamics: myosin on actin and rotary enzyme F1-ATPase
AFM allows the visualization of biological samples under physiological solution conditions, at high spatial resolution. However, captured images are limited to snapshots because it takes at least 30 seconds to capture an image, whereas biological phenomena are highly dynamic. To overcome this limitation, my group has developed high-speed AFM. The dynamic processes and structural dynamics of pro...
متن کاملOne rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolar.
F(1)-ATPase is a rotary molecular motor in which the central gamma-subunit rotates inside a cylinder made of alpha(3)beta(3)-subunits. The rotation is driven by ATP hydrolysis in three catalytic sites on the beta-subunits. How many of the three catalytic sites are filled with a nucleotide during the course of rotation is an important yet unsettled question. Here we inquire whether F(1) rotates ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2004
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.2004.04328.x