Exploration of environmental dynamics using intrinsic biological probe tryptophan is very important; however, it suffers from various difficulties. An alternative probe, kynurenine (KN), has been found to be an efficient probe for the ultrafast dynamics in the biological environment (Goswami et al.,  J. Phys. Chem. B., 114, 15236–15243). In the present study, we have investigated the efficacy of KN for the exploration of relatively slower dynamics of biologically relevant environments. A detailed investigation involving UV–Vis, steady-state/time-resolved fluorescence spectroscopy and Förster resonance energy transfer (FRET) studies on KN compared to a well-known solvation probe, H33258, a DNA-minor groove binder in a model nonionic reverse micelle reveals that ultrafast internal conversion associated with the hydrogen-bonding dynamics masks KN to become a dynamical reporter of the immediate environments of the probe.