To confirm this explanation, we also examined a different enzymatic reaction that does not involve charged moieties near the active site. For this example we chose the decarboxylation of l-apartate by the enzyme l-aspartate α-decarboxylase (AspDC), which has also been studied using QC models of varying size. Here, we consider only the C-C cleavage step, using a model consisting of 30 monomers (511 atoms), corresponding to a 5 Å radial cutoff around the active site of the relaxed crystal structure. This system has zero net charge but two ionic amino acids, which we placed together in a single fragment in order to avoid having any charged fragments.