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Previous kinetic models had assumed that the reaction medium was reacting atrandom and without a turnover associated to thermodynamics exchanges, with arigid active site on the enzyme. The experimental studies show that couplingfactor 1 (CF1) from spinach chloroplasts has latent ATPase activity, whichbecome expressed after heat-treatment and incubation with calcium. Thesigmoidal kinetics observed on the competitive effect of glycerol on watersaturating a protein, suggests that the role of the hydration shell in thecatalytic mechanism of the CF1-ATPase, modify the number of water moleculesassociated with the conformational turnover required for active site activity.It is assume that the water associated to the hydrophilic state of the enzymeproduces a fit-in of the substrate to form (ES), follow by the catalytic actionwith product formation (EP). This one induces the dissociation of water andincreases the hydrophobic attractions between R-groups. The latter, becomes theform of the enzyme interacting with water to form the dissociated free enzyme(E) and free product (P). Glycerol dependent suppression of the water dynamicson two interacting sites configuration shows a change in theH-bond-configuration. The thermodynamics modeling requires an energyexpenditure of about 4kcal/mol per each H-bond in turnover. Glycerol determineda turnover of 14 molecules of water released from the active sites to reach theinactive form of the enzyme. The entropy generated by turnover of the fit-inand -out substrate and product from the protein could be dissipated-out of theenzyme-water system itself. Coupling with the surrounding water clusters allowsto recreate H-bonds. This should involve a decrease in the number of H-bondspresent in the clusters. These changes in the mass action capability of thewater clusters could eventually become dissipated through a cooling effect.

The assay of the hydration shell dynamics on the turnover of the active site of CF1-ATPase