Journal of the American Society for Mass Spectrometry

, Volume 21, Issue 2, pp 268–277

Electron capture dissociation mass spectrometry of tyrosine nitrated peptides

Authors

  • Andrew W. Jones
    • School of BiosciencesUniversity of Birmingham
  • Victor A. Mikhailov
    • School of BiosciencesUniversity of Birmingham
  • Jesus Iniesta
    • Department of Physical ChemistryUniversity of Alicante
    • School of BiosciencesUniversity of Birmingham
Article

DOI: 10.1016/j.jasms.2009.10.011

Cite this article as:
Jones, A.W., Mikhailov, V.A., Iniesta, J. et al. J Am Soc Mass Spectrom (2010) 21: 268. doi:10.1016/j.jasms.2009.10.011

Abstract

In vivo protein nitration is associated with many disease conditions that involve oxidative stress and inflammatory response. The modification involves addition of a nitro group at the position ortho to the phenol group of tyrosine to give 3-nitrotyrosine. To understand the mechanisms and consequences of protein nitration, it is necessary to develop methods for identification of nitrotyrosine-containing proteins and localization of the sites of modification. Here, we have investigated the electron capture dissociation (ECD) and collision-induced dissociation (CID) behavior of 3-nitrotyrosine-containing peptides. The presence of nitration did not affect the CID behavior of the peptides. For the doubly-charged peptides, addition of nitration severely inhibited the production of ECD sequence fragments. However, ECD of the triply-charged nitrated peptides resulted in some singly-charged sequence fragments. ECD of the nitrated peptides is characterized by multiple losses of small neutral species including hydroxyl radicals, water and ammonia. The origin of the neutral losses has been investigated by use of activated ion (AI) ECD. Loss of ammonia appears to be the result of non-covalent interactions between the nitro group and protonated lysine side-chains.

Supplementary material

13361_2011_210200268_MOESM1_ESM.pdf (252 kb)
Supplementary material, approximately 258 KB.

Copyright information

© American Society for Mass Spectrometry 2010