ArticleJournal of the American Society for Mass Spectrometry2011
Transition metal ions: charge carriers that mediate the electron capture dissociation pathways of peptides.
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 14 papers.
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Who cites it
14 citing papers in PubMed.
- Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026Review
- From [2Mn2S] Diamond Cores to Butterfly Rhombs: Transformations That Highlight Alternating Peptide Binding Sites.Inorganic chemistry · 2024Article
- Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium.Journal of mass spectrometry : JMS · 2018Article
- Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein.Scientific reports · 2018Article
- Electron Transfer Dissociation and Collision-Induced Dissociation of Underivatized Metallated Oligosaccharides.Journal of the American Society for Mass Spectrometry · 2018Article
- Effects of acidic peptide size and sequence on trivalent praseodymium adduction and electron transfer dissociation mass spectrometry.Journal of mass spectrometry : JMS · 2017Article
- The Effects of Trivalent Lanthanide Cationization on the Electron Transfer Dissociation of Acidic Fibrinopeptide B and its Analogs.Journal of the American Society for Mass Spectrometry · 2016Article
- Difference of Electron Capture and Transfer Dissociation Mass Spectrometry on Ni(2+)-, Cu(2+)-, and Zn(2+)-Polyhistidine Complexes in the Absence of Remote Protons.Journal of the American Society for Mass Spectrometry · 2016Article
- The Competitive influence of Li+, Na+, K+, Ag+, and H+ on the fragmentation of a PEGylated polymeric excipient.Journal of the American Society for Mass Spectrometry · 2015Article
- Populations of metal-glycan structures influence MS fragmentation patterns.Journal of the American Society for Mass Spectrometry · 2015Article
- Mechanistic study on electron capture dissociation of the oligosaccharide-Mg²⁺ complex.Journal of the American Society for Mass Spectrometry · 2014Article
- Influence of metal-peptide complexation on fragmentation and inter-fragment hydrogen migration in electron transfer dissociation.Journal of the American Society for Mass Spectrometry · 2014Article
- Electron capture dissociation of trivalent metal ion-peptide complexes.Journal of the American Society for Mass Spectrometry · 2013Article
- Supercharging with trivalent metal ions in native mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
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6 authors.
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Abstract
Electron capture dissociation (ECD) of model peptides adducted with first row divalent transition metal ions, including Mn(2+), Fe(2+), Co(2+), Ni(2+), Cu(2+), and Zn(2+), were investigated. Model peptides with general sequence of ZGGGXGGGZ were used as probes to unveil the ECD mechanism of metalated peptides, where X is either V or W; and Z is either R or N. Peptides metalated with different divalent transition metal ions were found to generate different ECD tandem mass spectra. ECD spectra of peptides metalated by Mn(2+) and Zn(2+) were similar to those generated by ECD of peptides adducted with alkaline earth metal ions. Series of c-/z-type fragment ions with and without metal ions were observed. ECD of Fe(2+), Co(2+), and Ni(2+) adducted peptides yielded abundant metalated a-/y-type fragment ions; whereas ECD of Cu(2+) adducted peptides generated predominantly metalated b-/y-type fragment ions. From the present experimental results, it was postulated that electronic configuration of metal ions is an important factor in determining the ECD behavior of the metalated peptides. Due presumably to the stability of the electronic configuration, metal ions with fully-filled (i.e., Zn(2+)) and half filled (i.e., Mn(2+)) d-orbitals might not capture the incoming electron. Dissociation of the metal ions adducted peptides would proceed through the usual ECD channel(s) via "hot-hydrogen" or "superbase" intermediates, to form series of c-/z(•)- fragments. For other transition metal ions studied, reduction of the metal ions might occur preferentially. The energy liberated by the metal ion reduction would provide enough internal energy to generate the "slow-heating" type of fragment ions, i.e., metalated a-/y- fragments and metalated b-/y- fragments.
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