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Muscle contractile force is thought to be generated by ATP-induced conformational changes in myosin crossbridges. In the present study, we investigated the response to ATP binding of force-bearing, attached cross-bridges. For this investigation, skinned fibers, in which myosin heads were in part covalently crosslinked to thin filaments with a zero-length crosslinker, were prepared. Caged ATP [the P3-1-(2-nitro)phenylethyl ester of ATP] was then pulse-photolyzed in these crosslinked fibers, which retained ATP-induced "rigor" tension, and then the subsequent tension changes were followed at 14-16 degrees C and ionic strengths of 0.1-2 M. A rapid tension decrease was observed after the photolysis in the partially crosslinked fibers. The rate of the decrease was not any different from that in the uncrosslinked fibers compared at ionic strength of 0.2 M. This and other results thus indicate a kinetic similarity in the crosslinked and uncrosslinked crossbridges in response to ATP binding. These findings also suggest that ATP-induced structural changes take place in the attached crossbridges at a rate similar to that of the ATP-induced dissociation of crossbridges from thin filaments.

Tension relaxation induced by pulse photolysis of caged ATP in partially crosslinked fibers from rabbit psoas muscle.