The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Tandem Mass Spectrometry of Large Biomolecule Ions by Blackbody Infrared Radiative Dissociation
Abstract
A new method for the dissociation of large ions formed by electrospray ionization is demonstrated. Ions trapped in a Fourier transform mass spectrometer at pressures below 10(-)(8) Torr are dissociated by elevating the vacuum chamber to temperatures up to 215 °C. Rate constants for dissociation are measured and found to be independent of pressure below 10(-)(7) Torr. This indicates that the ions are activated by absorption of blackbody radiation emitted from the chamber walls. Dissociation efficiencies as high as 100% are obtained. There is no apparent mass limit to this method; ions as large as ubiquitin (8.6 kDa) are readily dissociated. Thermally stable ions, such as melittin 3+ (2.8 kDa), did not dissociate at temperatures up to 200 °C. This method is highly selective for low-energy fragmentation, from which limited sequence information can be obtained. From the temperature dependence of the dissociation rate constants, Arrhenius activation energies in the low-pressure limit are obtained. The lowest energy dissociation processes for the singly and doubly protonated ions of bradykinin are loss of NH(3) and formation of the b(2)/y(7) complementary pair, with activation energies of 1.3 and 0.8 eV, respectively. No loss of NH(3) is observed for the doubly protonated ion; some loss of H(2)O occurs. These results show that charge-charge interactions not only lower the activation energy for dissociation but also can dramatically change the fragmentation, most likely through changes in the gas-phase conformation of the ion. Dissociation of ubiquitin ions produces fragmentation similar to that obtained by IRMPD and SORI-CAD. Higher charge state ions dissociate to produce y and b ions; the primary fragmentation process for low charge state ions is loss of H(2)O.
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Citations
Cites
Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers.
Hillenkamp, F., Karas, M., Beavis, R. C., & Chait, B. T. (1991) · Analytical Chemistry · doi:10.1021/ac00024a716 · Cited by 1,930
Cited by
Fragmentation pathways of protonated peptides
Paizs, B., & Suhai, S. (2005) · Mass Spectrometry Reviews · doi:10.1002/mas.20024 · Cited by 1,118
Dongré, A. R., Jones, J. L., Somogyi, Á., & Wysocki, V. H. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9542193 · Cited by 894
‘Top down’ protein characterization via tandem mass spectrometry
Reid, G. E., & McLuckey, S. A. (2002) · Journal of Mass Spectrometry · doi:10.1002/jms.346 · Cited by 285
Rodriguez-Cruz, S. E., Jockusch, R. A., & Williams, E. R. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9911871 · Cited by 201
Self-citationKitova, E. N., Kitov, P. I., Bundle, D. R., & Klassen, J. S. (2001) · Glycobiology · doi:10.1093/glycob/11.7.605 · Cited by 59
Metadata
- Authors
- Price, W. D., Schnier, P. D., & Williams, E. R.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-03-01
- Volume
- 68
- Issue
- 5
- Pages
- 859-866
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2031498259
- Cited by
- 314
- References
- 1
- FWCI
- 15.75
- Type
- journal article
- Language
- en
- Open access
- closed
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