Reaction coordinate

tions compensates for the increase in free energy required to bend the stick. Reaction coordinate diagrams (right) show the energy consequences of complementarity to substrate versus complementarity to transition state (EP complexes are omitted). AGM, the difference between the transition-state energies of the uncatalyzed and catalyzed reactions, is contributed by the magnetic interactions between the stick and stickase. When the enzyme is complementary to the substrate (b), the ES complex is more stable and has less free energy in the ground state than substrate alone. The result is an increase in the activation energy.

reflects the need for superstructure to keep interacting groups properly positioned and to keep the cavity from collapsing.

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