Dissociation kinetics of singly protonated leucine enkephalin investigated by time-resolved photodissociation tandem mass spectrometry

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Title
Dissociation kinetics of singly protonated leucine enkephalin investigated by time-resolved photodissociation tandem mass spectrometry
Author(s)
Jeong Hee Moon; S H Yoon; Y J Bae; M S Kim
Bibliographic Citation
Journal of American Society for Mass Spectrometry, vol. 21, no. 7, pp. 1151-1158
Publication Year
2010
Abstract
The yields of post-source decay (PSD) and time-resolved photodissociation (PD) at 193 and 266 nm were measured for singly protonated leucine enkephalin ([YGGFL + H]+), a benchmark in the study of peptide ion dissociation, by using tandem time-of-flight mass spectrometry. The peptide ion was generated by matrix-assisted laser desorption ionization (MALDI) using 2,5-dihydroxybenzoic acid as the matrix. The critical energy (E0) and entropy (δS# at 1000 K) for the dissociation were determined by Rice-Ramsperger-Kassel-Marcus fit of the experimental data. MALDI was done for a mixture of YGGFL and Y6 and the plume temperature determined by the kinetic analysis of [Y6 + H]+ data were used to improve the precision of E0 and δS# for [YGGFL + H]+. E0 and δS# thus determined (E0 = 0.67 ± 0.08 eV, δS# = -24.4 ± 3.2 eu with 1 eu = 4.184 J K-1mol-1) were significantly different from those determined by blackbody infrared radiative dissociation (BIRD) (E0 = 1.10 eV, δS# = -14.9 eu), and by surface-induced dissociation (SID) (E0 = 1.13 eV, δS# = -10.3 eu). Analysis of the present experimental data with the SID kinetics (and BIRD kinetics also) led to an unrealistic situation where not only PSD and PD but also MALDI-TOF signals could not be detected. As an explanation for the discrepancy, it was suggested that transition-state switching occurs from an energy bottleneck (SID/BIRD) to an entropy bottleneck (PSD/PD) as the internal energy increases.
ISSN
1044-0305
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1016/j.jasms.2010.03.025
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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