2016
DOI: 10.1007/s41048-016-0032-5
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Thermodynamic aspects of ATP hydrolysis of actomyosin complex

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Cited by 10 publications
(9 citation statements)
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“…The molecular events that enable myosin to bind to actin in a post-hydrolysis state with bound ADP and P i are still a matter of debate [ 11 , 13 , 14 , 17 , 39 ]. The state is predicted to represent a high actin affinity conformation with the actin-binding cleft closed; however, it is different from the classical rigor state with the lever-arm in an up position [ 20 , 40 , 41 ].…”
Section: Introductionmentioning
confidence: 99%
“…The molecular events that enable myosin to bind to actin in a post-hydrolysis state with bound ADP and P i are still a matter of debate [ 11 , 13 , 14 , 17 , 39 ]. The state is predicted to represent a high actin affinity conformation with the actin-binding cleft closed; however, it is different from the classical rigor state with the lever-arm in an up position [ 20 , 40 , 41 ].…”
Section: Introductionmentioning
confidence: 99%
“…In particular, the P-A packing energy drives the P-ATPase to the transition state E 2 * P at which the energy-releasing step of dephosphorylation occurs. A similar reasoning of ''energy storage in dissociation'' has been proposed to explain the ATP hydrolysis cycle in linear ATP-driven motors such as the actomyosin system (Zhang and Feng 2016) as well as ABC transporters . In the words of P. Boyer who solved the mystery of rotatory ATP synthase, such a mechanism can be called ''binding change mechanism'' (Boyer 1998).…”
Section: Energy Of Atp Hydrolysismentioning
confidence: 78%
“…Resulting time courses of most involved reactants, including their length-dependency, are displayed in Figure A1 in Supplementary Material. The addressed interaction between ATP, ADP, and P i is known to influence the chemical potential (Zhang and Feng, 2016) or affinity (Allen and Orchard, 1987;Cooke, 2007;Hancock et al, 2005) of ATP, write µ ATP , which constitutes for the new state variable of phosphate dynamics. In a nutshell, the position of equilibrium (22) influences the amount of free Gibbs energy from ATP hydrolysis via…”
Section: B Atp Reaction Kineticsmentioning
confidence: 99%
“…where G • ATP ≈ −30 kJ/mol (Allen and Orchard, 1987;Cooke, 2007;Guynn and Veech, 1973;Rosing and Slater, 1972;Zhang and Feng, 2016) denotes the standard free enthalpy, R = 8.31 • 10 −3 kJ/(mol•K) the ideal gas constant, T = 303 K a temperature of 30 • C, and c 0 = 1 M the standard concentration. The latter serves as a normalization factor.…”
Section: B Atp Reaction Kineticsmentioning
confidence: 99%