Near-Edge Soft X-ray Absorption Mass Spectrometry of Protonated Melittin
(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.].
(Less)
- author
- organization
- publishing date
- 2018
- 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}}, }