Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 22, Issue 2, Pages 221-232Publisher
SPRINGER
DOI: 10.1007/s13361-010-0041-4
Keywords
Posttranslational modifications; PTMs; Nitration; Nitrosylation; Activation techniques; Fragmentation techniques; Electron transfer dissociation; ETD; Electron capture dissociation; ECD; Metastable atoms; Penning ionization; Peptide sequencing
Funding
- Protea Biosciences
- NSF BIO [0649757]
- NSF [CHE 0745590]
- Div Of Biological Infrastructure
- Direct For Biological Sciences [0649757] Funding Source: National Science Foundation
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The fragmentation behavior of nitrated and S-nitrosylated peptides were studied using collision induced dissociation (CID) and metastable atom-activated dissociation mass spectrometry (MAD-MS). Various charge states, such as 1+, 2+, 3+, 2-, of modified and unmodified peptides were exposed to a beam of high kinetic energy helium (He) metastable atoms resulting in extensive backbone fragmentation with significant retention of the post-translation modifications (PTMs). Whereas the high electron affinity of the nitrotyrosine moiety quenches radical chemistry and fragmentation in electron capture dissociation (ECD) and electron transfer dissociation (ETD), MAD does produce numerous backbone cleavages in the vicinity of the modification. Fragment ions of nitrosylated cysteine modifications typically exhibit more abundant neutral losses than nitrated tyrosine modifications because of the extremely labile nature of the nitrosylated cysteine residues. However, compared with CID, MAD produced between 66% and 86% more fragment ions, which preserved the labile -NO modification. MAD was also able to differentiate I/L residues in the modified peptides. MAD is able to induce radical ion chemistry even in the presence of strong radical traps and therefore offers unique advantages to ECD, ETD, and CID for determination of PTMs such as nitrated and S-nitrosylated peptides.
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