One of the paradigms of Zn2+ metallobiochemistry is that coordination of water to Zn2+ provides a mechanism of activation that involves lowering the pK(a) by approximately 7 pH units. This idea has become central to the development of mechanisms of action for zinc metalloproteins. However, the direct measurement of the pK(a) of water bound to Zn2+ in a metalloprotein has yet to be accomplished. Developing models for Zn2+-OH2 species has been a significant challenge, but we have utilized solid-state Zn-67 NMR spectroscopy as a means to characterize one of the few examples of water bound to mononuclear tetrahedral Zn2+: {[Tp(But,me)]Zn(OH2)}[HOB(C6F5)(3)]. The measured quadrupole coupling (C-q) constant is 4.3 MHz with an asymmetry parameter of eta(q) of 0.6. Likewise, due to the small value of C-q, anisotropic shielding also contributed to the observed Zn-67 NMR lineshape. As expected, the computed values of the magnetic resonance parameters depend critically on the nature of the anion. The predicted value of C-q for {[Tp(But,Me)]Zn(OH2)}[HOB(C6F5)(3)] is -4.88 MHz. We discuss the results of these calculations in terms of the nature of the anion, the local electrostatics, and its subsequent hydrogen bonding to [Tp(But,me)]Zn(OH2)(+).