Modeling the Weak pH Dependence of Proton-Coupled Electron Transfer for Tryptophan Derivatives

The oxidation of tryptophan (Trp) is an important step in many biological processes and often occurs by sequential or concerted proton-coupled electron transfer (PCET). The apparent rate constants for the photochemical oxidation of two Trp derivatives in water have been shown to be pH-independent at low pH and to exhibit weak pH dependence at higher pH. Herein, these systems are investigated with a general, multi-channel model that includes sequential and concerted mechanisms as well as various proton donors and acceptors. This model can reproduce the kinetic data for both Trp derivatives with physically meaningful parameters and suggests that the weak pH dependence may arise from the competition between OH^- and H₂O as proton acceptors in concerted PCET. Deprotonation of an ammonium group for one of the systems leads to a more complex pH dependence at higher pH. This work demonstrates the importance of considering multiple competing channels for the analysis of the pH dependence of apparent PCET rate constants.