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Article: Formation of peptide radical ions through dissociative electron transfer in ternary metal-ligand-peptide complexes

TitleFormation of peptide radical ions through dissociative electron transfer in ternary metal-ligand-peptide complexes
Authors
Issue Date2011
Citation
European Journal Of Mass Spectrometry, 2011, v. 17 n. 6, p. 543-556 How to Cite?
AbstractThe formation and fragmentation of odd-electron ions of peptides and proteins is of interest to applications in biological mass spectrometry. Gas-phase redox chemistry occurring during collision-induced dissociation of ternary metal-ligand-peptide complexes enables the formation of a variety of peptide radicals, including the canonical radical cations, M +·, radical dications, [M+H] 2+·, radical anions, [M-2H] -· and phosphorylated radical cations. In addition, odd-electron peptide ions with well-defined initial location of the radical site are produced through side-chain losses from the radical ions. Subsequent fragmentation of these species provides information regarding the role of charge and location of the radical site on the competition between radical-induced and proton-driven fragmentation of odd-electron peptide ions. This account summarizes current understanding of the factors that control the efficiency of the intramolecular electron transfer (ET) in ternary metal-ligand-peptide complexes resulting in formation of odd-electron peptide ions. Specifically, we discuss the effect of the metal center, the ligand and the peptide structure on the competition between the ET, proton transfer (PT) and loss of neutral peptide and neutral peptide fragments from the complex. Fundamental studies of the structures, stabilities and the energetics and dynamics of fragmentation of these complexes are also important for detailed molecular-level understanding of photosynthesis and respiration in biological systems. © IM Publications LLP 2011 All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/159308
ISSN
2015 Impact Factor: 1.011
2015 SCImago Journal Rankings: 0.380
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChu, IKen_HK
dc.contributor.authorLaskin, Jen_HK
dc.date.accessioned2012-08-16T05:48:34Z-
dc.date.available2012-08-16T05:48:34Z-
dc.date.issued2011en_HK
dc.identifier.citationEuropean Journal Of Mass Spectrometry, 2011, v. 17 n. 6, p. 543-556en_HK
dc.identifier.issn1469-0667en_HK
dc.identifier.urihttp://hdl.handle.net/10722/159308-
dc.description.abstractThe formation and fragmentation of odd-electron ions of peptides and proteins is of interest to applications in biological mass spectrometry. Gas-phase redox chemistry occurring during collision-induced dissociation of ternary metal-ligand-peptide complexes enables the formation of a variety of peptide radicals, including the canonical radical cations, M +·, radical dications, [M+H] 2+·, radical anions, [M-2H] -· and phosphorylated radical cations. In addition, odd-electron peptide ions with well-defined initial location of the radical site are produced through side-chain losses from the radical ions. Subsequent fragmentation of these species provides information regarding the role of charge and location of the radical site on the competition between radical-induced and proton-driven fragmentation of odd-electron peptide ions. This account summarizes current understanding of the factors that control the efficiency of the intramolecular electron transfer (ET) in ternary metal-ligand-peptide complexes resulting in formation of odd-electron peptide ions. Specifically, we discuss the effect of the metal center, the ligand and the peptide structure on the competition between the ET, proton transfer (PT) and loss of neutral peptide and neutral peptide fragments from the complex. Fundamental studies of the structures, stabilities and the energetics and dynamics of fragmentation of these complexes are also important for detailed molecular-level understanding of photosynthesis and respiration in biological systems. © IM Publications LLP 2011 All rights reserved.en_HK
dc.languageengen_US
dc.relation.ispartofEuropean Journal of Mass Spectrometryen_HK
dc.subject.meshElectron Transporten_HK
dc.subject.meshFree Radicals - chemistryen_HK
dc.subject.meshIons - chemistryen_HK
dc.subject.meshLigandsen_HK
dc.subject.meshMass Spectrometry - methodsen_HK
dc.subject.meshMetals - chemistryen_HK
dc.subject.meshPeptides - chemistryen_HK
dc.titleFormation of peptide radical ions through dissociative electron transfer in ternary metal-ligand-peptide complexesen_HK
dc.typeArticleen_HK
dc.identifier.emailChu, IK:ivankchu@hku.hken_HK
dc.identifier.authorityChu, IK=rp00683en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1255/ejms.1156en_HK
dc.identifier.pmid22274945-
dc.identifier.scopuseid_2-s2.0-84856251414en_HK
dc.identifier.hkuros203528en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84856251414&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue6en_HK
dc.identifier.spage543en_HK
dc.identifier.epage556en_HK
dc.identifier.isiWOS:000300967000002-
dc.identifier.scopusauthoridChu, IK=7103327484en_HK
dc.identifier.scopusauthoridLaskin, J=7102409836en_HK

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