Abstract Myosins are molecular motors that convert the chemical energy of ATP into mechanical work called a power stroke. Class II myosin engaged in muscle contraction is reported to show a “loose coupling phenomenon”, in which the number of power strokes is greater than the number of ATP hydrolyses. This phenomenon cannot be explained by the lever-arm hypothesis, which is currently accepted as a standard theory for myosin motility. In this paper, a model is proposed to reproduce the loose coupling phenomenon. The model is based on a mechanochemical process called “Driven by Detachment (DbD)” mechanism, which assumes that the energy of the power strokes originates from the potential energy generated by the attractive force between myosin and actin. During the docking process, the potential energy is converted into an intramolecular strain in a myosin molecule, which drives the power stroke after the myosin is firmly attached to an actin filament. The energy of ATP is used to temporarily reduce the attractive force and to increase the potential energy. Therefore, it is not directly linked to the power strokes. When myosin molecules work as an aggregate, the sliding movement of a myosin filament driven by the power strokes of some myosin heads makes other myosin heads that have completed their power strokes detach from the actin without consuming ATP. Under the DbD mechanism, these passively detached myosins can be again engaged in power strokes after the next attachment to actin. As a result, the number of power strokes becomes greater than the number of ATP hydrolyses, and the loose coupling phenomenon will be observed. A theoretical analysis indicates that the efficiency of converting the potential energy into intramolecular elastic energy determines the number of power strokes per each ATP hydrolysis. Computer simulations showed that the DbD mechanism actually produced the loose coupling phenomenon. A critical requirement for this mechanism is that ATP must preferentially facilitate the detachment of myosins that have completed their power strokes, but are still strongly attached to the actin. This requirement may be fulfilled by ATP hydrolysis tightly depending on the conformation of a myosin molecule.