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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Published on: April 28, 2022

Quantum behavior of water protons in protein hydration shell.

S E Pagnotta¹, F Bruni, R Senesi

¹Centro de Fisica des Materiales, Centro Mixto CSIC-UPV/EHU, Donostia-San Sebastian, Spain.

Biophysical Journal

|March 4, 2009

Summary

Quantum effects influence water proton movement on hydrated proteins. Experiments show proton delocalization, suggesting new insights into enzyme catalysis and proton transfer mechanisms.

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Area of Science:

Biophysics
Quantum Mechanics
Protein Dynamics

Background:

Understanding proton dynamics in hydrated proteins is crucial for biological processes.
Enzymatic catalysis often involves proton transfer, but the underlying mechanisms remain complex.
Quantum effects are increasingly recognized as potentially significant in biological systems.

Purpose of the Study:

To experimentally investigate quantum effects on water proton dynamics on protein surfaces.
To explore the role of proton delocalization in hydrated protein systems.
To assess the implications for enzymatic catalysis, specifically proton transfer.

Main Methods:

Broadband dielectric spectroscopy was employed to measure proton dynamics.
Deep inelastic neutron scattering (DINS) was used to probe water proton momentum distributions.
Comparative analysis of hydrogenated and deuterated protein samples was performed.

Main Results:

Dielectric spectroscopy revealed a reduced energy barrier in hydrogenated versus deuterated samples.
A significant, temperature-dependent isotopic ratio was observed, aligning with theoretical predictions.
Reanalyzed DINS data demonstrated characteristic proton delocalization in water at ambient temperatures.

Conclusions:

Experimental evidence supports the influence of quantum effects on water proton dynamics in hydrated proteins.
Proton delocalization is a key feature of water behavior on protein surfaces.
These findings have significant implications for understanding proton transfer in enzymatic catalysis, exemplified by lysozyme.