منابع مشابه
The unbinding of ATP from F1-ATPase.
Using molecular dynamics, we study the unbinding of ATP in F(1)-ATPase from its tight binding state to its weak binding state. The calculations are made feasible through use of interpolated atomic structures from Wang and Oster [Nature 1998, 396: 279-282]. These structures are applied to atoms distant from the catalytic site. The forces from these distant atoms gradually drive a large primary r...
متن کاملF1-ATPase-catalyzed synthesis of ATP from oleoylphosphate and ADP.
Purified preparations of F1-ATPase (ATP phosphohydrolase; EC 3.6.1.3) isolated from yeast mitochondria catalyze the reaction of oleoylphosphate with ADP to yield ATP and oleic acid. Formation of ATP is specifically inhibited by the F1-ATPase inhibitor 1799 and by dinitrophenol. In the presence of F1, dinitrophenol "uncouples" the synthase reaction by causing rapid hydrolysis of oleoylphosphate ...
متن کاملInhibition sites in F1-ATPase from bovine heart mitochondria.
High-resolution crystallographic studies of a number of inhibited forms of bovine F1-ATPase have identified four independent types of inhibitory site: the catalytic site, the aurovertin B-binding site, the efrapeptin-binding site and the site to which the natural inhibitor protein IF1 binds. Hitherto, the binding sites for other inhibitors, such as polyphenolic phytochemicals, non-peptidyl lipo...
متن کاملTemperature-sensitive reaction intermediate of F1-ATPase
F(1)-ATPase is a rotary molecular motor that makes 120 degrees stepping rotations, with each step being driven by a single-ATP hydrolysis. In this study, a new reaction intermediate of F(1)-ATPase was discovered at a temperature below 4 degrees C, which makes a pause at the same angle in its rotation as when ATP binds. The rate constant of the intermediate reaction was strongly dependent on tem...
متن کاملSingle molecule energetics of F1-ATPase motor.
Motor proteins are essential in life processes because they convert the free energy of ATP hydrolysis to mechanical work. However, the fundamental question on how they work when different amounts of free energy are released after ATP hydrolysis remains unanswered. To answer this question, it is essential to clarify how the stepping motion of a motor protein reflects the concentrations of ATP, A...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1989
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.43-1007