Alternative, more advanced, models of electrostatics have been implemented in new families of biomolecular force fields, of which the Charmm Drude and AMOEBA force fields are amongst the most extensively developed. Both include explicit representation of mutual polarization, and AMOEBA also incorporates a classical multipole representation of fixed electrostatics. These potential functions have been repeatedly shown to improve representation of electrostatic properties around biologically relevant moieties, and can improve the reliability and convergence properties of hybrid quantum mechanical/molecular mechanical (QM/MM) studies. Nevertheless, the accuracy advantages of polarizable force fields in the context of real protein environments are still poorly understood, and should be explored in systems where quantitatively accurate intramolecular electrostatics may be crucial to provide mechanistic insight. Biological catalysis is a particular focus in this regard as, in both naturallyoccurring and designed systems, enzyme active sites may pre-orient substrates and stabilize reaction transition states with focused electric fields or other electrostatic motifs. Although studies of the enzyme-catalyzed chemical reactions require QM/MM techniques, the reactant and product states can be studied efficiently with purely MM models, provided the underlying electrostatic model is sufficiently accurate to provide useful information on the active site environment.