Back Cover: Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations (Chem. Eur. J. 48/2016). Issue 48 (2nd November 2016)

• Record Type: Journal Article
• Authors: Scuderi, Debora; Bodo, Enrico; Chiavarino, Barbara; Fornarini, Simonetta; Crestoni, Maria Elisa
• Is Part Of: Chemistry. Volume 22:Issue 48(2016)
• Page Start: 17488
• Page End: 17488
• Publication Date: 2016-11-02
• Subjects: amino acids -- density functional calculations -- IR spectroscopy -- mass spectrometry -- post-translational modification; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201604434
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : 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. onpage 17239 ff.