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Electron Capture Dissociation Mass Spectrometry of Tyrosine Nitrated Peptides

Jones, Andrew W. and Mikhailov, Victor A. and Iniesta, Jesus and Cooper, Helen J. (2010) Electron Capture Dissociation Mass Spectrometry of Tyrosine Nitrated Peptides. Journal of the American Society for Mass Spectrometry, 21 (2). p. 268. ISSN 10440305

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URL of Published Version: http://dx.doi.org/10.1016/j.jasms.2009.10.011

Identification Number/DOI: doi:10.1016/j.jasms.2009.10.011

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 association (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.

Type of Work:Article
Date:2010 (Publication)
School/Faculty:Colleges (2008 onwards) > College of Life & Environmental Sciences
Department:School of Biosciences
Subjects:QP Physiology
Institution:University of Birmingham
Copyright Holders:American Society for Mass Spectrometry
ID Code:416
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