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Nolting, Dirk; Aziz, Emad F; Ottosson, Niklas; Faubel, Manfred; Hertel, Ingolf V; Winter, Bernd
Journal of the American Chemical Society, 11/2007, Letnik: 129, Številka: 45Journal Article
We demonstrate the applicability of X-ray photoelectron spectroscopy to obtain charge- and site-specific electronic structural information of biomolecules in aqueous solution. Changing the pH of an aqueous solution of lysine from basic to acidic results in nitrogen 1s and carbon 1s chemical shifts to higher binding energies. These shifts are associated with the sequential protonation of the two amino groups, which affects both charge state and hydrogen bonding to the surrounding water molecules. The N1s chemical shift is 2.2 eV, and for carbon atoms directly neighboring a nitrogen the shift for C1s is ∼0.4 eV. The experimental binding energies agree reasonably with our calculated energies of lysine( aq ) for different pH values.
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