Charge-site-dependent dissociation of hydrogen-rich radical peptide cations upon vacuum UV photoexcitation

James A. Madsen, Ryan R. Cheng, Tamer S. Kaoud, Kevin N. Dalby, Dmitrii E. Makarov, Jennifer S. Brodbelt

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Here, 193 nm vacuum ultraviolet photodissociation (VUVPD) was used to investigate the fragmentation of hydrogen-rich radical peptide cations generated by electron transfer reactions. VUVPD offers new insight into the factors that drive radical- and photon-directed processes. The location of a basic Arg site influences photon-activated C α-C(O) bond cleavages of singly charged peptide radical cations, an outcome attributed to the initial conformation of the peptide as supported by molecular dynamics simulated annealing and the population of excited states upon UV excitation. This hybrid ETD/VUVPD method was employed to identify phosphorylation sites of the kinase domain of human TRPM7/ChaK1.

Original languageEnglish
Pages (from-to)5374-5383
Number of pages10
JournalChemistry - A European Journal
Volume18
Issue number17
DOIs
StatePublished - Apr 23 2012

Funding

FundersFunder number
National Institute of General Medical SciencesR01GM059802
National Institute of General Medical Sciences

    Keywords

    • mass spectrometry
    • peptides
    • photodissociation
    • proteomics
    • radical ions

    ASJC Scopus subject areas

    • General Chemistry
    • Catalysis
    • Organic Chemistry

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