Electron-correlation-driven charge migration in oligopeptides

• Verfasst von: Kuleff, Alexander I. [VerfasserIn]
• Verfasst von: Lünnemann, Siegfried [VerfasserIn]
• Verfasst von: Cederbaum, Lorenz S. [VerfasserIn]
• Titel: Electron-correlation-driven charge migration in oligopeptides
• Verf.angabe: Alexander I. Kuleff, Siegfried Lünnemann, Lorenz S. Cederbaum
• Jahr: 2013
• Umfang: 6 S.
• Teil: volume:414
• Teil: year:2013
• Teil: month:03
• Teil: pages:100-105
• Teil: extent:6
• Fussnoten: Available online 14 March 2012 ; Gesehen am 30.06.2021
• Titel Quelle: Enthalten in: Chemical physics
• Ort Quelle: Amsterdam [u.a.] : Elsevier Science, 1973
• Jahr Quelle: 2013
• Band/Heft Quelle: 414(2013) vom: März, Seite 100-105
• DOI: doi:10.1016/j.chemphys.2012.02.019
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: C-terminally methylamidated dipeptide
• Sach-SW: Charge migration
• Sach-SW: Ionization spectra
• Sach-SW: Ultrafast electron dynamics
• K10plus-PPN: 1761601415

Abstract

Due to many-body effects an ultrafast removal of an electron from a molecule can trigger electron dynamics in which the created hole charge migrates throughout the system on a few-femtoseconds time scale. Here we report ab initio calculations of the positive-charge migration following inner-valence ionization of the C-terminally methylamidated dipeptide Gly-Gly-NH-CH3. To investigate the influence of the molecular symmetry on the process, two different conformations of the system are studied. Our results show that in both conformers the charge initially localized on the methylamine end of the system migrates to the remote glycine in only 5-6fs jumping thereby over an entire amino acid. Our computations also show that the symmetry of the system facilitates the process - a larger fraction of the charge migrates over a larger distance if the molecule is symmetric. Ionization spectra of both studied conformers are also reported.