Phillip Broadwith summarised briefly the ASAP JOC article by Simon and Goodman on the consequences of the geometry of hydrogen bonds during enzyme catalysis.
I might be wrong, but after having read the original article, I would put the emphasis slightly different.
Following the Hammond postulate, a certain similarity is expected for the geometry of the Ground State (GS) and Transition State (TS) for exothermic reactions, thus stabilisation of both states via one set of hydrogen bonds should not come as a surprise.
The authors of the JOC article assume that the optimal – most stabilising – hydrogen bond orientation is the same for GS and TS. Both energy levels are dropping, but the energy difference is still the barrier (the hill) between the two states.
The authors found that a suboptimal dihedral angle is a little less destabilising for the TS than for the GS. In other words, the overall barrier shrinks with the consequence that the enzymatic reaction becomes faster.
It is not directly my field, but how many enzyme transition states are exactly known (to my knowledge, the first one was around 2003, Science)?
Goodman and Simon write in their conclusion, that “Unlike water, enzymes can choose to orient their hydrogen bonds to stabilize the transition state slightly less well than is optimal, in order to stabilize the substrate much less well than is possible with the same number of hydrogen bonds.”
Maybe I missed the point, but does this necessarily exclude the possibility that the TS is actually well stabilised but slightly different in geometry than anticipated?