Abstract
Neutron diffraction analysis studies reported an isolated hydronium ion (H3O+) in the interior of d-xylose isomerase (XI) and phycocyanobilin-ferredoxin oxidoreductase (PcyA).
Using a quantum mechanical/molecular mechanical (QM/MM) approach, we analyzed stabilization of H3O+ by the protein environment. QM/MM calculations indicated that H3O+ was unstable in the PcyA crystal structure, releasing a proton to an H-bond partner His88, producing H2O and protonated His88.
On the other hand, H3O+ was stable in the XI crystal structure.
H-bond partners of isolated H3O+ would be practically limited to acidic residues such as aspartic and glutamic acids in the protein environment.