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"Dynamic Energy Landscape" of enzyme in Catalysis

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"These findings contrast with the traditional 'induced fit' hypothesis," Wright said. "One of the tenets of that hypothesis is that the binding of ligands induces a structural change that increases the complementary relationship between the ligand and the enzyme."

As the study points out, most proteins do not have rigid molecular structures but are structurally heterogeneous; the motion and plasticity in their structure allows them to achieve a far greater range of functions than would be possible with static structures.

However, despite considerable evidence that many enzymes are inherently flexible, the fundamental mechanisms by which protein fluctuations couple with catalytic function remain poorly understood. In the new conformational model, a small number of minor conformational sub-states that resemble the ligand-bound conformations are already present in solution. When the ligand binds to the minor sub-state, it causes an equilibrium shift so that the ligand-bound conformation becomes the new major sub-state.

"Our study can be placed in the broader context of the catalytic cycle," Wright said. "The results imply that for each of the intermediates in the catalytic cycle of DHFR, the lowest energy excited states are the most functionally relevant conformations. The enzyme structure responds to ligands by taking up a preferred ground-state conformation, but also samples other relevant conformations of higher energy, enabling it to rapidly advance to the next steps in catalysis. As ligands change, the energy landscape and the accessible states of the enzyme change in response. Consequently, this dynamic energy landscape efficiently funnels the enzyme along a specific kinetic path, where the number and heights of the barriers between consecutive conformations have been minimized."

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