Key result
The interaction of ADP with the myosin active center is a homogeneous process conforming to a simple two-step reaction mechanism, independent of the association state of the active centers.
The study demonstrates that ADP binding to skeletal muscle myosin follows a simple two-step reaction mechanism and that the two active sites in heavy meromyosin and myosin function identically and independently.
No immediate clinical implications for myosin-targeted therapies; leaves open translation to sarcomeric regulation in vivo.
The mechanism of interaction between ADP and the myosin active center has been studied using a transient kinetic technique. The results show that the interaction of ADP with the myosin active center is a homogeneous process independent of the association state of the active centers; namely, whether ADP interacts with the monomeric myosin subfragment-1, or with the dimeric forms heavy meromyosin and myosin. The kinetics of the interaction conforms to a simple two-step reaction mechanism for ADP binding. The kinetic and thermodynamic constants for this mechanism have been determined. In addition, analysis of the binding isotherm indicates that the two active sites in heavy meromyosin and myosin function as identical and independent sites.
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Stephen P. Chock (1981) studied this question. ADP interaction with myosin active center was evaluated on Kinetics and thermodynamics of ADP binding to myosin. The interaction of ADP with the myosin active center is a homogeneous process conforming to a simple two-step reaction mechanism, independent of the association state of the active centers.
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