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The Mechanism Behind Top-Down UVPD Experiments: Making Sense of Apparent Contradictions

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Specialty Chemistry
Date 2017 Jul 14
PMID 28702929
Citations 47
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Abstract

Top-down ultraviolet photodissociation (UVPD) allows greater sequence coverage than any other currently available method, often fracturing the vast majority of peptide bonds in whole proteins. At the same time, UVPD can be used to dissociate noncovalent complexes assembled from multiple proteins without breaking any covalent bonds. Although the utility of these experiments is unquestioned, the mechanism underlying these seemingly contradictory results has been the subject of many discussions. Herein, some fundamental considerations of photochemistry are briefly summarized within the context of a proposed mechanism that rationalizes the experimental results obtained by UVPD. Considerations for future instrument design, in terms of wavelength choice and power, are briefly discussed. Graphical Abstract ᅟ.

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References
1.
Lermyte F, Williams J, Brown J, Martin E, Sobott F . Extensive Charge Reduction and Dissociation of Intact Protein Complexes Following Electron Transfer on a Quadrupole-Ion Mobility-Time-of-Flight MS. J Am Soc Mass Spectrom. 2015; 26(7):1068-76. DOI: 10.1007/s13361-015-1124-z. View

2.
Yeh G, Sun Q, Meneses C, Julian R . Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores. J Am Soc Mass Spectrom. 2008; 20(3):385-93. DOI: 10.1016/j.jasms.2008.10.019. View

3.
Girod M, Sanader Z, Vojkovic M, Antoine R, MacAleese L, Lemoine J . UV photodissociation of proline-containing peptide ions: insights from molecular dynamics. J Am Soc Mass Spectrom. 2014; 26(3):432-43. DOI: 10.1007/s13361-014-1038-1. View

4.
Morrison L, Brodbelt J . 193 nm Ultraviolet Photodissociation Mass Spectrometry of Tetrameric Protein Complexes Provides Insight into Quaternary and Secondary Protein Topology. J Am Chem Soc. 2016; 138(34):10849-59. PMC: 5479422. DOI: 10.1021/jacs.6b03905. View

5.
Thompson M, Cui W, Reilly J . Fragmentation of singly charged peptide ions by photodissociation at lambda = 157 nm. Angew Chem Int Ed Engl. 2004; 43(36):4791-4. DOI: 10.1002/anie.200460788. View