F1-ATPase Dwell and Power Stroke Relationships
نویسندگان
چکیده
منابع مشابه
Electrostatic origin of the mechanochemical rotary mechanism and the catalytic dwell of F1-ATPase.
Understanding the nature of energy transduction in life processes requires a quantitative description of the energetics of the conversion of ATP to ADP by ATPases. Previous attempts to do so have provided an interesting insight but could not account for the rotary mechanism by a nonphenomenological structure/energy description. In particular it has been very challenging to account for the obser...
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 کاملTorsional elasticity and energetics of F1-ATPase.
F(o)F(1)-ATPase is a rotary motor protein synthesizing ATP from ADP driven by a cross-membrane proton gradient. The proton flow through the membrane-embedded F(o) generates the rotary torque that drives the rotation of the asymmetric shaft of F(1). Mechanical energy of the rotating shaft is used by the F(1) catalytic subunit to synthesize ATP. It was suggested that elastic power transmission wi...
متن کاملThe 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 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...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2018
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2018.09.078