Abstract
Hydrogen bonds with double minimum proton potential show so — called proton polarizabilities which are 1–2 orders of magnitude larger than usual polarizabilities due to distortion of electron systems. They cause continua in the IR spectra.
It is shown by an ab initio SCF treatment that H—bonded chains with multiminima proton potentials show still larger proton polarizabilities than single H—bonds. With a multiminima model proton potential it is shown that the proton polarizability increases with increasing number of minima and becomes up to four orders of magnitude larger than usual polarizabilities.
IR continua demonstrate that intramolecular H—bonded systems may show large proton polarizability. Many H—bonds between side chains of proteins show large proton polarizability. It is discussed that chains built up by such bonds would also show large proton polarizability since the proton motion within these bonds is coupled via proton dispersion forces. Finally it is demonstrated that H—bonded systems formed by side chains and several phosphates show large proton polarizability. The behavior of these systems is strongly cation and sometimes pH dependent.
Thus, all these systems are very effective proton wires which may be controlled by the cations present and sometimes by the pH.
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Zundel, G. (1988). Hydrogen - Bonded Systems as Proton Wires Formed by Side Chains of Proteins and by Side Chains and Phosphates.. In: Pullman, A., Jortner, J., Pullman, B. (eds) Transport Through Membranes: Carriers, Channels and Pumps. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 21. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3075-9_27
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DOI: https://doi.org/10.1007/978-94-009-3075-9_27
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