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...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 9(2002), Pt 6 vom: 01. Nov., Seite 342-6
1. Verfasser: Weik, Martin (VerfasserIn)
Weitere Verfasser: Bergès, Jacqueline, Raves, Maria L, Gros, Piet, McSweeney, Sean, Silman, Israel, Sussman, Joel L, Houée-Levin, Chantal, Ravelli, Raimond B G
Format: Aufsatz
Sprache:English
Veröffentlicht: 2002
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
LEADER 01000naa a22002652 4500
001 NLM121973875
003 DE-627
005 20231222194224.0
007 tu
008 231222s2002 xx ||||| 00| ||eng c
028 5 2 |a pubmed24n0407.xml 
035 |a (DE-627)NLM121973875 
035 |a (NLM)12409620 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Weik, Martin  |e verfasserin  |4 aut 
245 1 0 |a Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation 
264 1 |c 2002 
336 |a Text  |b txt  |2 rdacontent 
337 |a ohne Hilfsmittel zu benutzen  |b n  |2 rdamedia 
338 |a Band  |b nc  |2 rdacarrier 
500 |a Date Completed 07.01.2003 
500 |a Date Revised 10.12.2019 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a 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 
650 4 |a Comparative Study 
650 4 |a Evaluation Study 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Disulfides  |2 NLM 
650 7 |a Free Radicals  |2 NLM 
650 7 |a Proteins  |2 NLM 
700 1 |a Bergès, Jacqueline  |e verfasserin  |4 aut 
700 1 |a Raves, Maria L  |e verfasserin  |4 aut 
700 1 |a Gros, Piet  |e verfasserin  |4 aut 
700 1 |a McSweeney, Sean  |e verfasserin  |4 aut 
700 1 |a Silman, Israel  |e verfasserin  |4 aut 
700 1 |a Sussman, Joel L  |e verfasserin  |4 aut 
700 1 |a Houée-Levin, Chantal  |e verfasserin  |4 aut 
700 1 |a Ravelli, Raimond B G  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of synchrotron radiation  |d 1994  |g 9(2002), Pt 6 vom: 01. Nov., Seite 342-6  |w (DE-627)NLM09824129X  |x 1600-5775  |7 nnns 
773 1 8 |g volume:9  |g year:2002  |g number:Pt 6  |g day:01  |g month:11  |g pages:342-6 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_40 
912 |a GBV_ILN_350 
912 |a GBV_ILN_2005 
951 |a AR 
952 |d 9  |j 2002  |e Pt 6  |b 01  |c 11  |h 342-6