https://doi.org/10.1140/epjd/s10053-021-00147-y
Regular Article – Atomic and Molecular Collisions
The influence of the methionine residue on the dissociation mechanisms of photoionized methionine-enkephalin probed by VUV action spectroscopy
1
Deutsches Elektronen-Synchrotron DESY, Notkestrasse 85, 22607, Hamburg, Germany
2
Univ Lyon, Université Claude Bernard Lyon 1, Institut des Sciences Analytiques, CNRS UMR 5280, 5 rue de la Doua, 69100, Villeurbanne, France
3
Univ Lyon, Université Claude Bernard Lyon 1, Institut Lumière Matière, CNRS UMR 5306, 69622, Lyon, France
4
National Physical Laboratory, Hampton Road, TW11 0LW, Teddington, UK
5
Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
6
Institut für Röntgenphysik, Georg-August Universität Göttingen, Friedrich-Hund-Platz 1, 37077, Göttingen, Germany
a
simon.doerner@desy.de
j
sadia.bari@desy.de
Received:
31
January
2021
Accepted:
7
April
2021
Published online:
27
April
2021
VUV action spectroscopy has recently gained interest for the study of peptides and proteins. However, numerous aspects of the fundamental processes involved in the photodissociation are yet to be understood. It can, for example, be expected that sulfur-containing amino-acid residues have a significant impact on the dissociation processes following photoionization because of their potential involvement in the transport of electron holes in proteins. In order to investigate the influence of the sulfur-containing methionine residue on the VUV photodissociation of a small peptide a VUV action spectroscopy study of gas-phase protonated methionine-enkephalin and leucine-enkephalin in the photon energy range of 6–35 eV was performed. The results show that upon non-ionizing photoexcitation, the fragmentation patterns of the two peptides are nearly identical, whereas significant differences were observed upon photoionization. The differences between the fragment yields and the identified specific dissociation channels for methionine-enkephalin could be explained by the high electron hole affinity of sulfur, which efficiently directs the radical to the methionine side chain. Additionally, for both peptides the presence of the intact photoionized precursor ions was confirmed by their isotopic patterns and the stability of these species could be evaluated.
© The Author(s) 2021
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
