Chemo-Mechanical Coupling in F1-ATPase
نویسندگان
چکیده
منابع مشابه
Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis.
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. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hithe...
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F(1)-ATPase is a nanosized biological energy transducer working as part of F(o)F(1)-ATP synthase. Its rotary machinery transduces energy between chemical free energy and mechanical work and plays a central role in the cellular energy transduction by synthesizing most ATP in virtually all organisms. However, information about its energetics is limited compared to that of the reaction scheme. Act...
متن کاملChemomechanical coupling of F1-ATPase under hydrolysis conditions
F1-ATPase (F1) is the smallest rotary motor protein that couples ATP hydrolysis/synthesis to rotary motion in a highly reversible manner. F1 is unique compared with other motor proteins because of its high efficiency and reversibility in converting chemical energy into mechanical work. To determine the energy conversion mechanism of F1-ATPase, we developed a novel single-molecule manipulation t...
متن کاملMechanical modulation of catalytic power on F1-ATPase.
The conformational fluctuation of enzymes has a crucial role in reaction acceleration. However, the contribution to catalysis enhancement of individual substates with conformations far from the average conformation remains unclear. We studied the catalytic power of the rotary molecular motor F(1)-ATPase from thermophilic Bacillus PS3 as it was stalled in transient conformations far from a stabl...
متن کاملCoupling of Rotation and Catalysis in F1-ATPase Revealed by Single-Molecule Imaging and Manipulation
F(1)-ATPase is a rotary molecular motor that proceeds in 120 degrees steps, each driven by ATP hydrolysis. How the chemical reactions that occur in three catalytic sites are coupled to mechanical rotation is the central question. Here, we show by high-speed imaging of rotation in single molecules of F(1) that phosphate release drives the last 40 degrees of the 120 degrees step, and that the 40 ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2007
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.47.118