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Near-Edge Soft X-ray Absorption Mass Spectrometry of Protonated Melittin

Egorov, Dmitrii ; Bari, Sadia ; Boll, Rebecca ; Dörner, Simon ; Deinert, Sascha ; Techert, Simone ; Hoekstra, Ronnie ; Zamudio-Bayer, Vicente ; Lindblad, Rebecka LU and Bülow, Christine , et al. (2018) In Journal of the American Society for Mass Spectrometry 29(11). p.2138-2151
Abstract

We have investigated the photoionization and photofragmentation yields of gas-phase multiply protonated melittin cations for photon energies at the K-shell absorption edges of carbon, nitrogen, and oxygen. Two similar experimental approaches were employed. In both experiments, mass selected [melittin+qH]q+ (q=2–4) ions were accumulated in radiofrequency ion traps. The trap content was exposed to intense beams of monochromatic soft X-ray photons from synchrotron beamlines and photoproducts were analyzed by means of time-of-flight mass spectrometry. Mass spectra were recorded for fixed photon energies, and partial ion yield spectra were recorded as a function of photon energy. The combination of mass spectrometry and soft X-ray... (More)

We have investigated the photoionization and photofragmentation yields of gas-phase multiply protonated melittin cations for photon energies at the K-shell absorption edges of carbon, nitrogen, and oxygen. Two similar experimental approaches were employed. In both experiments, mass selected [melittin+qH]q+ (q=2–4) ions were accumulated in radiofrequency ion traps. The trap content was exposed to intense beams of monochromatic soft X-ray photons from synchrotron beamlines and photoproducts were analyzed by means of time-of-flight mass spectrometry. Mass spectra were recorded for fixed photon energies, and partial ion yield spectra were recorded as a function of photon energy. The combination of mass spectrometry and soft X-ray spectroscopy allows for a direct correlation of protein electronic structure with various photoionization channels. Non-dissociative single and double ionization are used as a reference. The contribution of both channels to various backbone scission channels is quantified and related to activation energies and protonation sites. Soft X-ray absorption mass spectrometry combines fast energy deposition with single and double ionization and could complement established activation techniques. [Figure not available: see fulltext.].

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Melittin, Photodissociation, Protonated proteins, Soft X-ray absorption, Soft X-ray spectroscopy
in
Journal of the American Society for Mass Spectrometry
volume
29
issue
11
pages
14 pages
publisher
Elsevier
external identifiers
  • pmid:30047073
  • scopus:85054893150
ISSN
1044-0305
DOI
10.1007/s13361-018-2035-6
language
English
LU publication?
yes
id
0525bb3a-4567-408c-bdad-c9caf8f6f8b5
date added to LUP
2018-10-30 09:43:21
date last changed
2024-01-30 00:28:33
@article{0525bb3a-4567-408c-bdad-c9caf8f6f8b5,
  abstract     = {{<p>We have investigated the photoionization and photofragmentation yields of gas-phase multiply protonated melittin cations for photon energies at the K-shell absorption edges of carbon, nitrogen, and oxygen. Two similar experimental approaches were employed. In both experiments, mass selected [melittin+qH]<sup>q+</sup> (q=2–4) ions were accumulated in radiofrequency ion traps. The trap content was exposed to intense beams of monochromatic soft X-ray photons from synchrotron beamlines and photoproducts were analyzed by means of time-of-flight mass spectrometry. Mass spectra were recorded for fixed photon energies, and partial ion yield spectra were recorded as a function of photon energy. The combination of mass spectrometry and soft X-ray spectroscopy allows for a direct correlation of protein electronic structure with various photoionization channels. Non-dissociative single and double ionization are used as a reference. The contribution of both channels to various backbone scission channels is quantified and related to activation energies and protonation sites. Soft X-ray absorption mass spectrometry combines fast energy deposition with single and double ionization and could complement established activation techniques. [Figure not available: see fulltext.].</p>}},
  author       = {{Egorov, Dmitrii and Bari, Sadia and Boll, Rebecca and Dörner, Simon and Deinert, Sascha and Techert, Simone and Hoekstra, Ronnie and Zamudio-Bayer, Vicente and Lindblad, Rebecka and Bülow, Christine and Timm, Martin and von Issendorff, Bernd and Lau, J. Tobias and Schlathölter, Thomas}},
  issn         = {{1044-0305}},
  keywords     = {{Melittin; Photodissociation; Protonated proteins; Soft X-ray absorption; Soft X-ray spectroscopy}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{2138--2151}},
  publisher    = {{Elsevier}},
  series       = {{Journal of the American Society for Mass Spectrometry}},
  title        = {{Near-Edge Soft X-ray Absorption Mass Spectrometry of Protonated Melittin}},
  url          = {{http://dx.doi.org/10.1007/s13361-018-2035-6}},
  doi          = {{10.1007/s13361-018-2035-6}},
  volume       = {{29}},
  year         = {{2018}},
}