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FEBS Lett. 1995 May 1;364(1):59-62.

Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases.

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INSERM U128, CNRS, Montpellier, France.


The myofibril is a good model to study the ATPase of the muscle fibre. When myofibrillar ATPase reaction mixtures are quenched in acid, there is a burst of Pi formation, due to AM.ADP.Pi or Pi, as shown in the scheme: AM+ATP<-->A.M.ATP<-->AM.ADP.Pi<-->AM.ADP+Pi<-->AM+ADP. Therefore, in the steady state, either AM.ADP.Pi or AM.ADP or both predominate. To determine which, we studied the reaction using a Pi binding protein (from E. coli) labeled with a fluorophore such that it is specific and sensitive to free Pi [Brune, M. et al. (1994) Biochemistry 33, 8262-8271]. We show that the Pi bursts with myofibrillar ATPases (calcium-activated or not, or crosslinked) are due entirely to protein bound Pi. Thus, with myofibrillar ATPases the AM.ADP.Pi state predominates.

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