Kinetics state diagram utility

The equilibrium constant for the TIM-catalyzed reaction is 22 in the direction of DHAP for the reactive, nonhydrated forms of DHAP and G3P [8] as a result, steady-state kinetics as well as the fates of substrate- and solvent-derived protons can be studied using either DHAP or G3P as substrate. In a series of landmark papers, Knowles and Albery quantitated the free energy profile for the reaction (Fig. 6.1) [37-42]. These studies utilized protiated, deuteriated, and tritiated forms of both DHAP and G3P in both unlabeled and tritiated water to follow the course of the transferred proton(s) during the course of the reaction. Several important conclusions were reached (i) for protiated substrates, the transition state for binding/release of G3P is the highest point on the energy diagram (ii) for tritiated... 

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