ArticleJournal of mass spectrometry : JMS2009
Correct identification of oxidized histidine residues using electron-transfer dissociation.
Article in Journal of mass spectrometry : JMS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A new ferrocene derivative blocks K-Ras localization and function by oxidative modification at His95.Life science alliance · 2023Article
- Photo-Oxidation of Therapeutic Protein Formulations: From Radical Formation to Analytical Techniques.Pharmaceutics · 2021Review
- 2-Oxo-Imidazole-Containing Dipeptides Play a Key Role in the Antioxidant Capacity of Imidazole-Containing Dipeptides.Antioxidants (Basel, Switzerland) · 2021Article
- Protein higher-order-structure determination by fast photochemical oxidation of proteins and mass spectrometry analysis.Nature protocols · 2020Article
- Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes.Journal of visualized experiments : JoVE · 2020Article
- Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions.Methods (San Diego, Calif.) · 2018Review
- Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2015Article
- Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS).Molecular & cellular proteomics : MCP · 2015Article
- Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Journal of the American Society for Mass Spectrometry · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Oxidative modification to the side chain of histidine can noticeably change the collision-induced dissociation (CID) pathways of peptides containing this oxidized residue. In cases where an oxidized peptide consists two or more isomers differing only in the site of modification, oxidation to histidine usually causes the other oxidized sites to be mis-assigned in CID spectra. These spectral misassignments can sometimes be avoided by using multiple stages of MS/MS (MS(n)) or via specially optimized liquid chromatographic separation conditions. In this manuscript, we demonstrate that these misassignments can be more readily and easily avoided by using electron-transfer dissociation (ETD) to dissociate the oxidized peptides. Furthermore, we find that the relative insensitivity of ETD to side-chain chemistry allows the extent of oxidative modification to be determined readily for peptide isomers having more than one site of oxidation. The current results along with previous studies of oxidized peptides suggest that ETD is probably a better technique than CID for obtaining correct sequence and modification information for oxidized peptides.
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