The dynamic phosphorescence Stokes shift (PSS) response of Zn(II)-substituted cytochrome c (ZnCytc) was detected using the time-resolved phosphorescence spectrum of the intrinsic Zn(II)-porphyrin chromophore, which senses the motions of the surrounding protein and hydration shell. The phosphorescence spectrum of ZnCytc exhibits resolved vibronic structure arising from in-plane deformations of the porphyrin macrocycle, as is also observed in the absorption and fluorescence spectra. As the emission time increases, the phosphorescence spectrum shifts to the red without incurring a significant change in vibronic structure or line shape, so the shift arises from dynamic solvation, the reorganizational motions of the protein and solvent that occur in response to formation of the first excited triplet state. A correlation time of 294 ± 14 μs was obtained from a single-exponential fit to the time dependence of the mean emission frequency of the T(0,0) peak in the phosphorescence spectrum. This time scale is consistent with a diffusive sampling of the native structure's minimum due to global or collective conformational fluctuations. We suggest that studies of the PSS response sensed in proteins by an intrinsic probe will be informative of protein and hydration-shell dynamics over the microsecond-millisecond time regimes associated with biological function.