All hBChE states along the normal reaction retain the dynamical proton transfer. In the free form, the Michaelis complex, and the TI1 state, it is equally likely to have a proton on either external or internal Glu. The EP state shows a preference for the protonated external Glu, while it is the other way around for the TI2 and the acyl-enzyme. In contrast, binding of OP inhibitors echothiophate and soman abolish the possibility of observing the protonated internal Glu.