Thermodynamics and kinetics of the FoF1-ATPase: application of the probability isotherm

What is it about?

Earlier experimental data were interpreted to indicate stoichiometric 'slippage' between gamma-shaft rotation of the F1-ATPase and chemical hydrolysis or synthesis of ATP. Numerical solution of the Probability Isotherm incorporating such hypothetical slippage shows that this explanation is unsatisfactory. Instead, we suggest that the data indicate that the internal work of overcoming rotatory friction within the isolated enzyme is approximately half of the free energy change associated with ATP hydrolysis.

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Why is it important?

It illustrates the power of application of the Probability Isotherm to establish consistency between thermodynamics and kinetics in the interpretation of experimental data. It incidentally shows - by explicit, simple, kinetic examples - the inapplicability of the commonly invoked expectations of the school of Linear Non-Equilibrium Thermodynamics (LNET) to such problems.

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