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Enzymes utilize protein architectures to create highly specialized structuralmotifs that can greatly enhance the rates of complex chemical transformations.Here we use experiments, combined with ab initio simulations that exactlyinclude nuclear quantum effects, to show that a triad of strongly hydrogenbonded tyrosine residues within the active site of the enzyme ketosteroidisomerase (KSI) facilitates quantum proton delocalization. This delocalizationdramatically stabilizes the deprotonation of an active site tyrosine residue,resulting in a very large isotope effect on its acidity. When an intermediateanalog is docked, it is incorporated into the hydrogen bond network, givingrise to extended quantum proton delocalization in the active site. Theseresults shed light on the role of nuclear quantum effects in the hydrogen bondnetwork that stabilizes the reactive intermediate of KSI, and the behavior ofprotons in biological systems containing strong hydrogen bonds.

Quantum delocalization of protons in the hydrogen bond network of an enzyme active site