ArticleJournal of the American Society for Mass Spectrometry2009
Time-resolved photodissociation study of singly protonated peptides with a histidine residue generated by matrix-assisted laser desorption ionization: dissociation rate constant and internal temperature.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Expansion cooling in the matrix plume is under-recognized in MALDI mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Changes in dissociation efficiency and kinetics of peptide ions induced by basic residues and their mechanistic implication.Journal of the American Society for Mass Spectrometry · 2011Article
- A comparative study of in- and post-source decays of peptide and preformed ions in matrix-assisted laser desorption ionization time-of-flight mass spectrometry: effective temperature and matrix effect.Journal of the American Society for Mass Spectrometry · 2010Article
- Dissociation kinetics of singly protonated leucine enkephalin investigated by time-resolved photodissociation tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Product ion yields in post-source decay and time-resolved photodissociation at 193 and 266 nm were measured for some peptide ions with a histidine residue ([HF(6) + H](+), [F(6)H + H](+), and [F(3)HF(3) + H](+)) formed by matrix-assisted laser desorption ionization (MALDI). Compared with similar data for peptide ions without any basic residue reported previously, significant reduction in dissociation efficiency was observed. Internal temperatures (T) of the peptide ions and their dissociation kinetic parameters-the critical energy (E(0)) and entropy (DeltaS(double dagger))-were determined by the method reported previously. Slight decreases in E(0), DeltaS(double dagger), and T were responsible for the histidine effect-reduction in dissociation rate constant. Regardless of the presence of the residue, DeltaS(double dagger) was far more negative than previous quantum chemical results. Based on this, we propose the existence of transition structures in which the nitrogen atoms in the histidine residue or at the N-terminus coordinate to the reaction centers. Reduction in T in the presence of a histidine residue could not be explained based on popular models for ion formation in MALDI, such as the gas-phase proton transfer model.
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