2j18
From Proteopedia
| 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 17:58:19 2008'' |
Revision as of 15:58, 21 February 2008
|
CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW 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
2J18 is a Single protein structure of sequence from Leptoxyphium fumago with , , , and as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Known structural/functional Site: . 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 17:58:19 2008
Categories: Chloride peroxidase | Leptoxyphium fumago | Single protein | Beitlich, T. | Kuhnel, K. | Schlichting, I. | Schulze-Briese, C. | Shoeman, R L. | BR | HEM | MAN | MN | NAG | Chloride | Glycoprotein | Heme | Iron | Manganese | Metal-binding | Oxidoreductase | Peroxidase | Pyrrolidone carboxylic acid
