Fe+ chemical ionization of peptides
- 1 February 1993
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Society for Mass Spectrometry
- Vol. 4 (2) , 106-110
- https://doi.org/10.1016/1044-0305(93)85065-6
Abstract
Laser-desorbed peptide neutral molecules were allowed to react with Fe+ in a Fourier transform mass spectrometer, using the technique of laser desorption/chemical ionization. The Fe+ ions are formed by laser ablation of a steel target, as well as by dissociative charge-exchange ionization of ferrocene with Ne+. Prior to reaction with laser-desorbed peptide molecules, Fe+ ions undergo 20–100 thermalizin collisions with xenon to reduce the population of excited-state metal ion species. The Fe+ ions that have not experienced thermalizing collisions undergo charge exchange with peptide molecules. Iron ions that undergo thermalizing collisions before they are allowed to react with peptides are found to undergo charge exchange and to form adduct species [M + Fe+] and fragment ions that result from the loss of small, stable molecules, such as H2O, CO, and CO2, from the metal ion-peptide complex.Keywords
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