Abstract:
Proton transfer reactions occur along the confinement structures with unique water molecules. These confinement structures consist of transient dynamical interactions that serve as proton transfer pathways. The confinement proton solvation in water has become a focus. Therefore, to have a platform to study and identify these confinement structure dynamics with interactions is desired. In response, we demonstrate the hybrid approach utilizing small to medium angle X-ray/neutron scattering (SAXS/SANS) contrast variation technique and high-resolution molecular dynamics simulations is a promising means to probe the interfacial/internal interactions between a protein hydrate structure and the ligand/water molecules’ binding pathway. To clarify the mechanism, cytochrome P450 proteins are good targets because it is noticeable that protein interior cavities play an important role in P450 function. Beside regular structure characterizations, the ligand binding protein process was monitored by in situ (operando) SAXS and SANS. We first identified the internal structure dynamics of the protein, which open/close a heme-site channel structure changes upon ligand binding. We examined their biological function and found the protein internal hydrate substructures with open/close states determine the enzyme activity. This study presents a unique platform for the study of transient interface interactions between ligand/water and enzymes, as well as encapsulating enzymes into zeolite imidazole Frameworks (ZIFs).
Keywords – Protonation, Deprotonation, Water Solvation, Nanoporous.
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