ArticleJournal of the American Society for Mass Spectrometry2012
S-to-αC radical migration in the radical cations of Gly-Cys and Cys-Gly.
Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 28 citations in OpenAlex.
- Chromophore Optimization in Organometallic Au(III) Cys Arylation of Peptides and Proteins for 266 nm Photoactivation.Analytical chemistry · 2024Article
- Near-UV Photodissociation of Tryptic Peptide Cation Radicals. Scope and Effects of Amino Acid Residues and Radical Sites.Journal of the American Society for Mass Spectrometry · 2017Article
- Gas-phase reactivity of peptide thiyl (RS•), perthiyl (RSS•), and sulfinyl (RSO•) radical ions formed from atmospheric pressure ion/radical reactions.Journal of the American Society for Mass Spectrometry · 2013Article
- The radical ion chemistry of S-nitrosylated peptides.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The radical cations of Cys-Gly and Gly-Cys were studied using ion-molecule reactions (IMR), infrared multiple-photon dissociation (IRMPD) spectroscopy, and density functional theory (DFT) calculations. Homolytic cleavage of the S-NO bond of nitrosylated precursors generated radical cations with the radical site initially located on the sulfur atom. Time-resolved ion-molecule reactions showed that radical site migration via hydrogen atom transfer (HAT) occurred much more quickly in Gly-Cys(•+) than in Cys-Gly(•+). IRMPD and DFT calculations indicated that for Gly-Cys, the radical migrated from the sulfur atom to the α-carbon of glycine, which is lower in energy than the sulfur radical (-53.5 kJ/mol). This migration does not occur for Cys-Gly because the glycine α-carbon is higher in energy than the sulfur radical (10.3 kJ/mol). DFT calculations showed that the highest energy barriers for rearrangement are 68.2 kJ/mol for Gly-Cys and 133.8 kJ/mol for Cys-Gly, which is in agreement with both the IMR and IRMPD data and explains the HAT in Gly-Cys.
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