Photoleucine Survives Backbone Cleavage by Electron Transfer Dissociation. A Near-UV Photodissociation and Infrared Multiphoton Dissociation Action Spectroscopy Study

0461787 - ÚOCHB 2017 RIV US eng J - Journal Article
Shaffer, C. J. - Martens, J. - Marek, Aleš - Oomens, J. - Tureček, F.
Photoleucine Survives Backbone Cleavage by Electron Transfer Dissociation. A Near-UV Photodissociation and Infrared Multiphoton Dissociation Action Spectroscopy Study.
Journal of the American Society for Mass Spectrometry. Roč. 27, č. 7 (2016), s. 1176-1185. ISSN 1044-0305. E-ISSN 1879-1123
Institutional support: RVO:61388963
Keywords : peptide ions * electron transfer dissociation * photoleucine label * near-UV photodissociation * infrared multiphoton dissociation action spectroscopy
Subject RIV: CF - Physical ; Theoretical Chemistry
Impact factor: 2.786, year: 2016

We report a combined experimental and computational study aimed at elucidating the structure of N-terminal fragment ions of the c type produced by electron transfer dissociation of photo-leucine (L*) peptide ions GL*GGKX. The c (4) ion from GL*GGK is found to retain an intact diazirine ring that undergoes selective photodissociation at 355 nm, followed by backbone cleavage. Infrared multiphoton dissociation action spectra point to the absence in the c (4) ion of a diazoalkane group that could be produced by thermal isomerization of vibrationally hot ions. The c (4) ion from ETD of GL*GGK is assigned an amide structure by a close match of the IRMPD action spectrum and calculated IR absorption. The energetics and kinetics of c (4) ion dissociations are discussed.
Permanent Link: http://hdl.handle.net/11104/0261370