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N‑Acetylglycine Cation Tautomerization Enabled by the Peptide Bond

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journal contribution
posted on 17.09.2015, 00:00 by Jaroslav Kocisek, Dariusz Grzegorz Piekarski, Rudy Delaunay, Bernd A. Huber, Lamri Adoui, Fernando Martín, Manuel Alcamí, Patrick Rousseau, Alicja Domaracka, Janina Kopyra, Sergio Díaz-Tendero
We present a combined experimental and theoretical study of the ionization of N-acetylglycine molecules by 48 keV O6+ ions. We focus on the single ionization channel of this interaction. In addition to the prompt fragmentation of the N-acetylglycine cation, we also observe the formation of metastable parent ions with lifetimes in the microsecond range. On the basis of density functional theory calculations, we assign these metastable ions to the diol tautomer of N-acetylglycine. In comparison with the simple amino acids, the tautomerization rate is higher because of the presence of the peptide bond. The study of a simple biologically relevant molecule containing a peptide bond allows us to demonstrate how increasing the complexity of the structure influences the behavior of the ionized molecule.