Tuesday, April 21, 2015

Calibrating a ruler for hydrogen bond lengths

I have just finished a paper with Bijyalaxmi Athokpam and Sai  Ramesh,
Isotopic fractionation in proteins as a measure of hydrogen bond length

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.

I welcome any comments or suggestions.

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