2v1k
From Proteopedia
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caption="2v1k, resolution 1.25Å" /> | caption="2v1k, resolution 1.25Å" /> | ||
'''CRYSTAL STRUCTURE OF FERROUS DEOXYMYOGLOBIN AT PH 6.8'''<br /> | '''CRYSTAL STRUCTURE OF FERROUS DEOXYMYOGLOBIN AT PH 6.8'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 2V1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional | + | 2V1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hem Binding Site For Residue A 1154'>AC1</scene>, <scene name='pdbsite=AC2:So4 Binding Site For Residue A 1156'>AC2</scene>, <scene name='pdbsite=AC3:So4 Binding Site For Residue A 1157'>AC3</scene>, <scene name='pdbsite=AC4:Gol Binding Site For Residue A 1158'>AC4</scene> and <scene name='pdbsite=AC5:Gol Binding Site For Residue A 1159'>AC5</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1K OCA]. |
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| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17565988 17565988] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:00:55 2008'' |
Revision as of 09:00, 31 January 2008
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CRYSTAL STRUCTURE OF FERROUS DEOXYMYOGLOBIN 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
2V1K is a Single protein structure of sequence from Equus caballus with , and as ligands. Known structural/functional Sites: , , , and . 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 Thu Jan 31 11:00:55 2008
Categories: Equus caballus | Single protein | Andersson, K.K. | Gorbitz, C.H. | Hersleth, H.P. | GOL | HEM | SO4 | Haem | Heme | Iron | Metal-binding | Monooxygenase | Muscle protein | Oxygen activation | Oxygen transport | Transport
