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Back Cover: Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations (Chem. Eur. J. 48/2016)
Author(s) -
Scuderi Debora,
Bodo Enrico,
Chiavarino Barbara,
Fornarini Simonetta,
Crestoni Maria Elisa
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201604434
Subject(s) - chemistry , sulfenic acid , deprotonation , cysteine , infrared multiphoton dissociation , sulfinic acid , infrared spectroscopy , tandem mass spectrometry , thiol , mass spectrometry , combinatorial chemistry , organic chemistry , ion , enzyme , chromatography
Redox signaling is triggered by post‐translational modifications at the cysteine thiol target. Cysteine residues in sulfenic, sulfinic and sulfonic forms are key intermediates in the redox‐switch chemistry of proteins. The deprotonated species were thoroughly characterized by an integrated approach combining tandem mass spectrometry, action IR spectroscopy and ab initio molecular dynamics simulations. Vibrational signatures mark the progressive cysteine sulfur oxidation and modulation of the deprotonation site (from carboxylic group in cysteine sulfenic acid to sulfonic group in the highest oxidized species). More information can be found in the Full Paper by M. E. Crestoni et al. on page 17239 ff.