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A scientific review discusses biochemistry and theory of proton-coupled electron transfer. It discusses that the amino acid radical environments of tryptophan and tyrosine are elaborated for a handful of proteins that utilize these amino acids for proton-coupled electron transfer (PCET). It focuses on tryptophan and tyrosine radicals as exemplars due to their relative simplicity, ubiquity, and close partnership with inorganic cofactors, while PCET occurs in biology via many different electron and proton donors along with involving many different substrates. The review has decided to discuss this organization for a few reasons, such as to highlight the rich PCET landscape within proteins containing these radicals and to emphasize that proteins are not just passive scaffolds that organize metallic charge transfer cofactors.
Migliore et al. (Tue,) studied this question.