Potential crossing position in electron transfer of a doubly charged ion and an alkali metal target measured using thermometer molecule W(CO)6

Hayakawa, Shigeo; Minami, Kaori; Iwamoto, Kaoru; Toyoda, Michisato; Ichihara, Toshio; Nagao, Hirofumi

doi:10.1016/j.ijms.2007.07.015

Cited by 13 publications

(16 citation statements)

References 38 publications

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“…Collisional electron transfer from a Cs atom can be described by an energy balance equation (ΔE, Equation 1), which contains the ion vertical recombination energy, RE v (ion), the Cs ionization energy, IE(Cs)=3.894 eV, a Coulomb term for the repulsive potential of the charge-reduced peptide ion and Cs cation in the product channel, and the attractive ion-induced dipole potential in the reactant channel at critical distance R c where electron transfer takes place [62]. Positive ΔE means that the electron transfer is exothermic.…”

Section: Electron Attachment Energeticsmentioning

confidence: 99%

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Moss

Chung

Wyer

et al. 2011

J. Am. Soc. Mass Spectrom.

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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 lowenergy 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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Section: Electron Attachment Energeticsmentioning

confidence: 99%

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Moss

Chung

Wyer

et al. 2011

J. Am. Soc. Mass Spectrom.

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“…In the present instrument, a quadrupole lens doublet was newly mounted and the conversion dynode of the detector was changed from the flat type used in the previous instrument [39,46] to a curved type. A schematic of the modified instrument is shown in Figure 1.…”

Section: Tandem Mass Spectrometry For High-energy Collision Induced Dmentioning

confidence: 99%

“…By assuming that the interaction region is twice of 6.8 ϫ 10 -10 m of the length at the Landau-Zener potential crossing evaluated for the Cs target [39], the interaction time between the collision partners is estimated to be 3.8 ϫ 10 -14 s. A period for dissociation was estimated from the length of 230 cm between the exit of the target chamber and the entrance of the MS-II is 6.5 s. This period is much shorter than the reaction time in the LE-ETD. Although the electron binding energies of 0.63 eV to be the electron affinity of the fluoranthene is much smaller than that of 3.89 eV of the ionization energy of the Cs, the difference of internal energies depositing to the charge reduced species between HE-ETD and LE-ETD is affected by charge-induced dipole interaction in the entrance channel of the electrontransfer as discussed in the previous papers [38,39]. While these differences exist, the similar result between the HE-ETD and the LE-ETD is supposed due to the electron-transfer process of bound electrons in both processes.…”

Section: Comparison Of the He-etd Using The Alkali Metal Target With mentioning

confidence: 99%

“…N-C␣ bond cleavages induced by electron-transfer processes of multiply charged peptides upon collision with alkali metals have been reported by Hvelplund and coworkers [32][33][34][35][36][37]. The mechanism of HE-ETD of doubly-charged ions on collision with alkali metal targets were elucidated by using thermometer molecules W(CO) 6 [38,39]. Recently, the result of electron-transfer process in the HE collision of the doubly-protonated phosphopeptides [(YGGMHRQET(p)VDC) ϩ 2H] 2ϩ (1) with the Cs target has been reported [40].…”

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confidence: 97%

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High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

Hayakawa

Matsumoto

Hashimoto

et al. 2010

J. Am. Soc. Mass Spectrom.

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Post-translational modifications (PTMs) of proteins are important in the activation, localization, and regulation of protein function in vivo. The usefulness of electron capture dissociation (ECD) and electron-transfer dissociation (ETD) in tandem mass spectrometry (MS/MS) using low-energy (LE) trap type mass spectrometer is associated with no loss of a labile PTM group regarding peptide and protein sequencing. The experimental results of high-energy (HE) collision induced dissociation (CID) using the Xe and Cs targets and LE-ETD were compared for doubly-phosphorylated peptides TGFLT(p)EY(p)VATR (1). Although HE-CID using the Xe target did not provide information on the amino acid sequence, HE-CID using the Cs target provided all the z-type ions without loss of the phosphate groups as a result of HE-ETD process, while LE-ETD using fluoranthene anion gave only z-type ions from z 5 to z 11 . The difference in the results of HE-CID between the Xe and Cs targets demonstrated that HE-ETD process with the Cs target took place much more dominantly than collisional activation. The difference between HE-ETD using Cs targets and LE-ETD using the anion demonstrated that mass discrimination was much weaker in the high-energy process. HE-ETD was also applied to three other phosphopeptides YGGMHRQEX(p)VDC (2: X ϭ S, 3: X ϭ T, 4: X ϭ Y). The HE-CID spectra of the doubly-protonated phosphopeptides () of 2, 3, and 4 using the Cs target showed a very similar feature that the c-type ions from c 7 to c 11 and the z-type ions from z 7 to z 11 were formed via N-C␣ bond cleavage without a loss of the phosphate group. (J Am Soc Mass Spectrom 2010, 21, 1482-1489) © 2010 American Society for Mass Spectrometry P ost-translational modifications (PTMs) of proteins are important in vivo, especially, reversible protein phosphorylation, principally localized on serine, threonine, or tyrosine residues, is one of the most important and well-studied. Phosphorylations play crucial roles in the regulation of cellular processes such as cell cycle, cell growth, apoptosis, and signal transduction [1,2]. Although the mass analysis of phosphorylated proteins and peptides has become possible since the development of electrospray ionization (ESI) technique [3], the determination of phosphorylated positions has not yet been achieved by the most popular dissociation method, namely, a low-energy collisionally activated dissociation (LE-CAD) performed by using the tandem mass spectrometry (MS/ MS) [4]. Electron capture dissociation (ECD) using a Fourier transform ion cyclotron resonant mass spectrometer (FT-ICR-MS) [5][6][7][8] and electron-transfer dissociation (ETD) using a linear trap mass spectrometer [9,10] can provide information on c-and z-type ions [11,12] produced via N-C␣ backbone cleavage with no loss of labile PTM groups, such as phosphate and sulfate groups [13,14]. The N-C␣ backbone cleavage is different from other fragmentations brought about by collisional activation or infrared photoexcitation of closedshell cations [15]. The charge reduced p...

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“…35) Di erences between the deposition of internal energy induced by collisional activation and electron transfer were investigated using W(CO) 6 2+ ions on collision with a rare gas and with an alkali metal target. 36,37) e internal energy deposition in collisionally activated dissociation (CAD) evaluated with a rare gas target was broad and decreased with increasing internal energy. On the contrary, internal energy depositions evaluated with alkali metal targets were very narrow and centered at a particular energy.…”

Section: Introductionmentioning

confidence: 99%

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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Potential crossing position in electron transfer of a doubly charged ion and an alkali metal target measured using thermometer molecule W(CO)6

Cited by 13 publications

References 38 publications

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

Dipole-Guided Electron Capture Causes Abnormal Dissociations of Phosphorylated Pentapeptides

High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides

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

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