Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation
Irradiation of proteins with intense X-ray radiation produced by third-generation synchrotron sources generates specific structural and chemical alterations, including breakage of disulfide bonds and decarboxylation. In this paper, disulfide bond lengths in irradiated crystals of the enzyme Torpedo...
| Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 9(2002), Pt 6 vom: 01. Nov., Seite 342-6 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2002
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| Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation |
| Schlagworte: | Comparative Study Evaluation Study Journal Article Research Support, Non-U.S. Gov't Disulfides Free Radicals Proteins |
| Zusammenfassung: | Irradiation of proteins with intense X-ray radiation produced by third-generation synchrotron sources generates specific structural and chemical alterations, including breakage of disulfide bonds and decarboxylation. In this paper, disulfide bond lengths in irradiated crystals of the enzyme Torpedo californica acetylcholinesterase are examined based on quantum simulations and on experimental data published previously. The experimental data suggest that one disulfide bond elongates by approximately 0.7 A upon X-ray irradiation as seen in a series of nine data sets collected on a single crystal. Simulation of the same bond suggests elongation by a similar value if a disulfide-radical anion is formed by trapping an electron. The absorption spectrum of a crystal irradiated under similar conditions shows a peak at approximately 400 nm, which in aqueous solution has been attributed to disulfide radicals. The results suggest that the formation of disulfide radicals in protein crystals owing to X-ray irradiation can be observed experimentally, both by structural means and by absorption spectroscopy |
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| Beschreibung: | Date Completed 07.01.2003 Date Revised 10.12.2019 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1600-5775 |