2v1e
From Proteopedia
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'''CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8''' | '''CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8''' | ||
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[[Category: Gorbitz, C H.]] | [[Category: Gorbitz, C H.]] | ||
[[Category: Hersleth, H P.]] | [[Category: Hersleth, H P.]] | ||
| - | [[Category: | + | [[Category: Ferryl]] |
| - | [[Category: | + | [[Category: Haem]] |
| - | [[Category: | + | [[Category: Heme]] |
| - | [[Category: | + | [[Category: Hydroxy radical]] |
| - | [[Category: | + | [[Category: Iron]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Monooxygenase]] |
| - | [[Category: | + | [[Category: Muscle protein]] |
| - | [[Category: | + | [[Category: Oxygen activation]] |
| - | [[Category: | + | [[Category: Oxygen transport]] |
| - | [[Category: | + | [[Category: Peroxidase]] |
| - | [[Category: | + | [[Category: Reaction intermediate]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:08:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr | + | |
Revision as of 20:08, 16 April 2008
CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8
Overview
High resolution crystal structures of myoglobin in the pH range 5.2-8.7 have been used as models for the peroxide-derived compound II intermediates in heme peroxidases and oxygenases. The observed Fe-O bond length (1.86-1.90 A) is consistent with that of a single bond. The compound II state of myoglobin in crystals was controlled by single-crystal microspectrophotometry before and after synchrotron data collection. We observe some radiation-induced changes in both compound II (resulting in intermediate H) and in the resting ferric state of myoglobin. These radiation-induced states are quite unstable, and compound II and ferric myoglobin are immediately regenerated through a short heating above the glass transition temperature (<1 s) of the crystals. It is unclear how this influences our compound II structures compared with the unaffected compound II, but some crystallographic data suggest that the influence on the Fe-O bond distance is minimal. Based on our crystallographic and spectroscopic data we suggest that for myoglobin the compound II intermediate consists of an Fe(IV)-O species with a single bond. The presence of Fe(IV) is indicated by a small isomer shift of delta = 0.07 mm/s from Mossbauer spectroscopy. Earlier quantum refinements (crystallographic refinement where the molecular-mechanics potential is replaced by a quantum chemical calculation) and density functional theory calculations suggest that this intermediate H species is protonated.
About this Structure
2V1E is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O., Hersleth HP, Uchida T, Rohr AK, Teschner T, Schunemann V, Kitagawa T, Trautwein AX, Gorbitz CH, Andersson KK, J Biol Chem. 2007 Aug 10;282(32):23372-86. Epub 2007 Jun 12. PMID:17565988 Page seeded by OCA on Wed Apr 16 23:08:31 2008
