High-energy electron transfer dissociation of protonated amino acids

Hayakawa, Shigeo; Ukezono, Kazuya; Fujihara, Akimasa

doi:10.1016/j.ijms.2015.06.016

Cited by 2 publications

(1 citation statement)

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“…1(g) Charge inversion mass spectrometry using alkali metal targets for singly protonated peptides and amino acids provide information on radical traps in the dissociation mechanism of the charge reduced doublet state peptides, as evidenced by a computational study. [54][55][56][57] For multiply charged peptides upon collision with alkali metals, N-C α bond cleavage induced by electron transfer processes have been reported by Hvelplund et al 58) A combined experimental and computational study of the e ect of proline in model dipeptides, i.e., Pro-Gly and Gly-Pro was performed. 55) Gas-phase protonated peptide ions were discharged by collision with potassium or cesium atoms at 3 keV collision energies, and the peptide radical intermediates and their dissociation products were analyzed following collisional ionization to anions.…”

Section: Charge Inversion Mass Spectrometrymentioning

confidence: 97%

Study of Ion Dynamics by Electron Transfer Dissociation: Alkali Metals as Targets

Hayakawa

2017

Mass Spectrometry

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High energy collision processes for singly charged positive ions using an alkali metal target are con rmed, as a charge inversion mass spectrometry, to occur by electron transfers in successive collisions and the dissociation processes involve the formation of energy-selected neutral species from near-resonant neutralization with alkali metal targets. A doubly charged thermometer molecule was made to collide with alkali metal targets to give singly and doubly charged positive ions. e internal energy resulting from the electron transfer with the alkali metal target was very narrow and centered at a particular energy. is narrow internal energy distribution can be attributed to electron transfer by Landau-Zener potential crossing between the precursor ion and an alkali metal atom, and the coulombic repulsion between singly charged ions in the exit channel. A large cross section of more than 10 −14 cm 2 was estimated for high-energy electron transfer dissociation (HE-ETD). Doubly protonated phosphorylated peptides obtained by electrospray ionization were collided with Xe and Cs targets to give singly and doubly charged positive ions. Whereas doubly charged fragment ions resulting from CAD were dominant in the case of the Xe target, singly charged fragment ions resulting from ETD were dominant with the Cs target. HE-ETD using the Cs target provided all of the z-type ions by N-C α bond cleavage without the loss of the phosphate groups. e results demonstrate that HE-ETD with an alkali metal target allowed the position of phosphorylation and the amino acid sequence of peptides with post translational modi cations (PTM) to be determined.

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