Molecular step(s) of force generation: temperature-perturbation experiments on muscle fibres.

The steady active muscle force is reduced, but the force generation induced by a standard temperature jump becomes 2-3 fold faster with increased inorganic phosphate level, [Pi]. The increase in the rate of force generation also exhibits saturation at higher [Pi] levels and the relation is hyperbolic. These observations are consistent with a kinetic scheme where rapid Pi release by actomyosin crossbridges in muscle is preceded by the force generation step. Such a scheme accounts for the sigmoidal temperature dependence of steady active force and its sensitivity to [Pi]. The [Pi] dependence of force recovery after stretch (positive strain) is also hyperbolic, suggesting that the "pre Pi-release force generation step" is strain-sensitive--as expected. However, length-release (negative strain) force transients are not [Pi] sensitive indicating an asymmetry, but its significance and also the kinetic step underlying force recovery from negative strain remain unclear.