ArticleJournal of the American Society for Mass Spectrometry2011
Dipole-guided electron capture causes abnormal dissociations of phosphorylated pentapeptides.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- Multimodal Tandem Mass Spectrometry Techniques for the Analysis of Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2022Article
- Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update.Analytical chemistry · 2019Review
- Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium.Journal of mass spectrometry : JMS · 2018Article
- Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Mass spectrometry reviews · 2018Review
- Toward a Rational Design of Highly Folded Peptide Cation Conformations. 3D Gas-Phase Ion Structures and Ion Mobility Characterization.Journal of the American Society for Mass Spectrometry · 2016Article
- Ground and Excited-Electronic-State Dissociations of Hydrogen-Rich and Hydrogen-Deficient Tyrosine Peptide Cation Radicals.Journal of the American Society for Mass Spectrometry · 2016Article
- Probing the electron capture dissociation mass spectrometry of phosphopeptides with traveling wave ion mobility spectrometry and molecular dynamics simulations.Journal of the American Society for Mass Spectrometry · 2015Article
- Electron transfer reduction of the diazirine ring in gas-phase peptide ions. On the peculiar loss of [NH4O] from photoleucine.Journal of the American Society for Mass Spectrometry · 2015Article
- Collision-induced dissociation of diazirine-labeled peptide ions. Evidence for Brønsted-acid assisted elimination of nitrogen.Journal of the American Society for Mass Spectrometry · 2014Article
- Electron transfer dissociation of photolabeled peptides. Backbone cleavages compete with diazirine ring rearrangements.Journal of the American Society for Mass Spectrometry · 2013Article
- Cation recombination energy/coulomb repulsion effects in ETD/ECD as revealed by variation of charge per residue at fixed total charge.Journal of the American Society for Mass Spectrometry · 2013Article
- Renaissance of cation-radicals in mass spectrometry.Mass spectrometry (Tokyo, Japan) · 2013Article
- The early life of a peptide cation-radical. Ground and excited-state trajectories of electron-based peptide dissociations during the first 330 femtoseconds.Journal of the American Society for Mass Spectrometry · 2012Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electron transfer and capture mass spectra of a series of doubly charged ions that were phosphorylated pentapeptides of a tryptic type (pS,A,A,A,R) showed conspicuous differences in dissociations of charge-reduced ions. Electron transfer from both gaseous cesium atoms at 100 keV kinetic energies and fluoranthene anion radicals in an ion trap resulted in the loss of a hydrogen atom, ammonia, and backbone cleavages forming complete series of sequence z ions. Elimination of phosphoric acid was negligible. In contrast, capture of low-energy electrons by doubly charged ions in a Penning ion trap induced loss of a hydrogen atom followed by elimination of phosphoric acid as the dominant dissociation channel. Backbone dissociations of charge-reduced ions also occurred but were accompanied by extensive fragmentation of the primary products. z-Ions that were terminated with a deaminated phosphoserine radical competitively eliminated phosphoric acid and H(2)PO(4) radicals. A mechanism is proposed for this novel dissociation on the basis of a computational analysis of reaction pathways and transition states. Electronic structure theory calculations in combination with extensive molecular dynamics mapping of the potential energy surface provided structures for the precursor phosphopeptide dications. Electron attachment produces a multitude of low lying electronic states in charge-reduced ions that determine their reactivity in backbone dissociations and H- atom loss. The predominant loss of H atoms in ECD is explained by a distortion of the Rydberg orbital space by the strong dipolar field of the peptide dication framework. The dipolar field steers the incoming electron to preferentially attach to the positively charged arginine side chain to form guanidinium radicals and trigger their dissociations.
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