Journal of the American Society for Mass Spectrometry

, Volume 16, Issue 6, pp 880–882

Electron transfer dissociation of peptide anions

Authors

    • Department of ChemistryUniversity of Virginia
  • Jeffrey Shabanowitz
    • Department of ChemistryUniversity of Virginia
  • Donald F. Hunt
    • Department of ChemistryUniversity of Virginia
    • the Department of Pathology, Health Sciences CenterUniversity of Virginia
  • John E. P. Syka
    • Engineering Physics ProgramUniversity of Virginia
    • Thermo Electron
Short Communication

DOI: 10.1016/j.jasms.2005.01.015

Cite this article as:
Coon, J.J., Shabanowitz, J., Hunt, D.F. et al. J Am Soc Mass Spectrom (2005) 16: 880. doi:10.1016/j.jasms.2005.01.015

Abstract

Ion/ion reactions of multiply deprotonated peptide anions with xenon radical cations result in electron abstraction to generate charge-reduced peptide anions containing a free-radical site. Peptide backbone cleavage then occurs by hydrogen radical abstraction from a backbone amide N to facilitate cleavage of the adjacent C-C bond, thereby producing a- and x-type product ions. Introduction of free-radical sites to multiply charged peptides allows access to new fragmentation pathways that are otherwise too costly (e. g., lowers activation energies). Further, ion/ion chemistry, namely electron transfer reactions, presents a rapid and efficient means of generating odd-electron multiply charged peptides; these reactions can be used for studying gas-phase chemistries and for peptide sequence analysis.

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© American Society for Mass Spectrometry 2005