The rate constants for typical concerted proton-coupled electron transfer (PCET) reactions depend on the vibronic coupling between the diabatic reactant and product states. The form of the vibronic coupling is different for electronically adiabatic and nonadiabatic reactions, which are associated with hydrogen atom transfer (HAT) and electron proton transfer (EPT) mechanisms, respectively. Most PCET rate constant expressions rely on the Condon approximation, which assumes that the vibronic coupling is independent of the nuclear coordinates of the solute and the solvent or protein. Herein we test the Condon approximation for PCET vibronic couplings. The dependence of the vibronic coupling on molecular geometry is investigated for an open and a stacked transition state geometry of the phenoxyl-phenol self-exchange reaction. The calculations indicate that the open geometry is electronically nonadiabatic, corresponding to an EPT mechanism that involves significant electronic charge redistribution, while the stacked geometry is predominantly electronically adiabatic, corresponding primarily to an HAT mechanism. Consequently, a single molecular system can exhibit both HAT and EPT character. The dependence of the vibronic coupling on the solvent or protein configuration is examined for the soybean lipoxygenase enzyme. The calculations indicate that this PCET reaction is electronically nonadiabatic with a vibronic coupling that does not depend significantly on the protein environment. Thus, the Condon approximation is shown to be valid for the solvent and protein nuclear coordinates but invalid for the solute nuclear coordinates in certain PCET systems. These results have significant implications for the calculation of rate constants, as well as mechanistic interpretations, of PCET reactions.