Coincidence studies of O 2−, O − and electron formation in electron-stripping of cationic biomolecules by molecular oxygen
In high-energy collisions between protonated biomolecules (amino acids, peptides and proteins) and molecular oxygen, electron-stripping of the cations occurs, i.e., they increase their charge state by one unit. The fate of the stripped electron depends on the cation under study. We have measured the...
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Published in | International journal of mass spectrometry Vol. 214; no. 1; pp. 57 - 62 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
15.02.2002
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Subjects | |
Online Access | Get full text |
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Summary: | In high-energy collisions between protonated biomolecules (amino acids, peptides and proteins) and molecular oxygen, electron-stripping of the cations occurs, i.e., they increase their charge state by one unit. The fate of the stripped electron depends on the cation under study. We have measured the negative recoils coincident with the electron-stripped ions to be O
2
−, O
−, and a free electron (which might be a result of autodetachment from an excited state of O
2
−). The ratio of the O
2
− recoils to electrons decreases in the following order:
[
Lys+9
H]
10+>[
Ubi+7
H]
8+>[
GS+2
H]
3+>
TyrH
2+,
PheH
2+
, in accordance with decreasing interaction times (Lys: lysozyme, Ubi: ubiquitine, GS: gramicidin S, Tyr: tyrosine, Phe: phenylalanine). |
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ISSN: | 1387-3806 1873-2798 |
DOI: | 10.1016/S1387-3806(01)00555-3 |