Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 20, Issue 8, Pages 1522-1529Publisher
SPRINGER
DOI: 10.1016/j.jasms.2009.04.008
Keywords
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Funding
- Korea Research Foundation, Republic of Korea
- Ministry of Education, Science and Technology, Republic of Korea [M10645010002-06N4501-00,210]
- Ministry of Education, Science and Technology, Republic of Korea
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Product ion yields in post-source decay and time-resolved photodissociation at 193 and 266 rim were measured for some peptide ions with a histidine residue ([HF6 + H](+) [F6H + H](+), and [F3HF3 + H](+)) formed by matrix-assisted laser desorption ionization (MALDI). Compared with similar data for peptide ions without my 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 (Delta S-double dagger)-were determined by the method reported previously. Slight decreases in E-0, Delta S-double dagger, and T were responsible for the histidine effect-reduction in dissociation rate constant. Regardless of the presence of the residue, Delta S-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. (J Am Soc Mass Spectrom 2009, 20, 1522-1529) (C) 2009 American Society for Mass Spectrometry
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