Isotopic fractionation in proteins as a measure of hydrogen bond length

Abstract

If a deuterated molecule containing strong intramolecular hydrogen bonds is placed in a hydrogenated solvent it may preferentially exchange deuterium for hydrogen. This preference is due to the difference between the vibrational zero-point energy for hydrogen and deuterium. It is found that the associated fractionation factor $\Phi$ is correlated with the strength of the intramolecular hydrogen bonds. This correlation has been used to determine the length of the H-bonds (donor-acceptor separation) in a diverse range of enzymes and has been argued to support the existence of short low-barrier H-bonds. Starting with a potential energy surface based on a simple diabatic state model for H-bonds we calculate $\Phi$ as a function of the proton donor-acceptor distance $R$. For numerical results, we use a parameterization of the model for symmetric O-H.... O bonds. We consider the relative contributions of the O-H stretch vibration, O-H bend vibrations (both in plane and out of plane), tunnelling splitting effects at finite temperature, and the secondary geometric isotope effect. We compare our total $\Phi$ as a function of $R$ with NMR experimental results for enzymes, and in particular with an empirical parametrisation $\Phi (R)$, used previously to determine bond lengths.

Final version, accepted for publication in Journal of Chemical Physics. Minor changes, including more extensive discussion of relevant of model to proteins

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Cited by in corpus (4)

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• Accelerating equilibrium isotope effect calculations: I. Stochastic thermodynamic integration with respect to mass