ArticleJournal of the American Society for Mass Spectrometry2009
Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Free-energy studies reveal a possible mechanism for oxidation-dependent inhibition of MGL.Scientific reports · 2016Article
- Key Residues of Outer Membrane Protein OprI Involved in Hexamer Formation and Bacterial Susceptibility to Cationic Antimicrobial Peptides.Antimicrobial agents and chemotherapy · 2015Article
- Cys34 adducts of reactive oxygen species in human serum albumin.Chemical research in toxicology · 2012Article
- Novel oxidative modifications in redox-active cysteine residues.Molecular & cellular proteomics : MCP · 2011Article
- Formation, reactivity, and detection of protein sulfenic acids.Chemical research in toxicology · 2010Review
- Chemical approaches to detect and analyze protein sulfenic acids.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We investigated the formation of hydroxyl radical (OH(*)) and H(2)O(2) mediated oxidation products of a synthetic peptide, HCSAGIGRS, which is an active site sequence motif of protein tyrosine phosphatase 1B (PTP1B). We determined that a novel cysteine sulfinamide HC[S(O)N]SAGIGRS is produced in the oxidation reaction by Fenton reagents (Fe(+2)/H(2)O(2)) as well as by H(2)O(2). These products were characterized by tandem mass spectrometry experiments on both singly and doubly charged precursor ions. MS(3) experiments using an ion trap instrument as well as LC-MS/MS experiments using a quadrupole time-of-flight (Q-TOF) instrument demonstrated that HC[S(O)N]SAGIGRS is not a water loss product of cysteine sulfinic acid [HC(SO(2)H)SAGIGRS]. We also obtained data from tandem mass spectrometry experiments that provided evidence for the existence of stable cysteine sulfenic acid [HC(SOH)SAGIGRS] in solution. A mechanism for the formation of the cysteine sulfinamide product is proposed based on the above experimental results. The preparation and identification of cysteine sulfinamide in this study may provide insight into the mechanism of both OH(*) and H(2)O(2) induced oxidation reactions of protein tyrosine phosphatases.
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