2j19: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
The X-ray crystallographic analysis of redox-active systems may be | The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed. | ||
==About this Structure== | ==About this Structure== | ||
| Line 18: | Line 18: | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Schulze-Briese, C.]] | [[Category: Schulze-Briese, C.]] | ||
[[Category: Shoeman, R | [[Category: Shoeman, R L.]] | ||
[[Category: BR]] | [[Category: BR]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| Line 34: | Line 34: | ||
[[Category: pyrrolidone carboxylic acid]] | [[Category: pyrrolidone carboxylic acid]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:15 2008'' | ||
Revision as of 15:58, 21 February 2008
|
FERROUS CHLOROPEROXIDASE (HIGH DOSE DATA SET)
Overview
The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed.
About this Structure
2J19 is a Single protein structure of sequence from Leptoxyphium fumago with NAG, MAN, MN, BR and HEM as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Known structural/functional Site: AC1. Full crystallographic information is available from OCA.
Reference
Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography., Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I, J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:17211068
Page seeded by OCA on Thu Feb 21 17:58:15 2008
