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Recently, observed large values of 'step size' in in vivo muscle contraction1), 2) and in vitro actomyosin motility assays3)-5) have raised new questions about the nature of coupling in biological systems. It has been experimentally demonstrated7) that multiple working strokes occur during the hydrolysis of one ATP molecule. It is difficult to explain these observations by conventional enzyme kinetics. In this paper, we propose a novel enzymatic mechanism (the 'coupling ratio constraint' mechanism). By 'free energy mixing' between the two coupled degrees of freedom, we can explain the mechanism underlying the large values of step size and the multiple working strokes per ATP hydrolyzed observed in muscle. We predict that myosin would behave in an unconventional manner during the multiple working strokes. This prediction can be tested experimentally. Finally, we propose that 'thermal interference', similar to quantum interference20)(but of different physical origin) is involved in the observed phenomenon.

Involvement of "Thermal Interference" in the Multiple Working Strokes Per Hydrolyzed ATP Observed in Muscle Contraction.