Characterization of Tyrosine Nitration and Cysteine Nitrosylation Modifications by Metastable Atom-Activation Dissociation Mass Spectrometry |
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Authors: | Shannon L Cook Glen P Jackson |
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Institution: | Center for Intelligent Chemical Instrumentation, Department of Chemistry and Biochemistry, Ohio University, Athens, OH 45701-2979, USA. |
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Abstract: | 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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