ArticleJournal of the American Society for Mass Spectrometry2004
Fragmentation of protonated ions of peptides containing cysteine, cysteine sulfinic acid, and cysteine sulfonic acid.
Article in Journal of the American Society for Mass Spectrometry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 50 citations in OpenAlex.
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- Insights into the binding sites of organometallic ruthenium anticancer compounds on peptides using ultra-high resolution mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Capturing labile sulfenamide and sulfinamide serum albumin adducts of carcinogenic arylamines by chemical oxidation.Analytical chemistry · 2013Article
- Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates.Free radical biology & medicine · 2012Article
- Negative ion fragmentation of cysteic acid containing peptides: cysteic acid as a fixed negative charge.Journal of the American Society for Mass Spectrometry · 2011Article
- Site-selective fragmentation of peptides and proteins at quinone-modified cysteine residues investigated by ESI-MS.Analytical chemistry · 2010Article
- Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B.Journal of the American Society for Mass Spectrometry · 2009Article
- Correct identification of oxidized histidine residues using electron-transfer dissociation.Journal of mass spectrometry : JMS · 2009Article
- Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases.Journal of the American Society for Mass Spectrometry · 2007Article
- Improved sequencing of oxidized cysteine and methionine containing peptides using electron transfer dissociation.Journal of the American Society for Mass Spectrometry · 2007Article
- The effect of histidine oxidation on the dissociation patterns of peptide ions.Journal of the American Society for Mass Spectrometry · 2007Article
- Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences.Applied and environmental microbiology · 2005Article
- Computational investigation and hydrogen/deuterium exchange of the fixed charge derivative tris(2,4,6-trimethoxyphenyl) phosphonium: implications for the aspartic acid cleavage mechanism.Journal of the American Society for Mass Spectrometry · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oxidation of the sulfhydryl group in cysteine to sulfenic acid, sulfinic acid, and sulfonic acid in proteins is important in a number of enzymatic processes. In this study we examined the fragmentation of four peptides containing cysteine, cysteine sulfinic acid (Cys-SO(2)H), and cysteine sulfonic acid (Cys-SO(3)H) in an ion-trap mass spectrometer. Our results show that the presence of a Cys-SO(2)H in a peptide leads to preferential cleavage of the amide bond at the C-terminal side of the oxidized cysteine residue. The results are important for the determination of the site of the cysteine oxidation and might be useful for the sequencing of cysteine-containing peptides.
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