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2v1j

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[[Image:2v1j.gif|left|200px]]
[[Image:2v1j.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2v1j |SIZE=350|CAPTION= <scene name='initialview01'>2v1j</scene>, resolution 1.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2v1j", creates the "Structure Box" on the page.
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|SITE= <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>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2v1j| PDB=2v1j | SCENE= }}
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|RELATEDENTRY=[[1azi|1AZI]], [[1bje|1BJE]], [[1dwr|1DWR]], [[1dws|1DWS]], [[1dwt|1DWT]], [[1gjn|1GJN]], [[1hrm|1HRM]], [[1hsy|1HSY]], [[1npf|1NPF]], [[1npg|1NPG]], [[1nz2|1NZ2]], [[1nz3|1NZ3]], [[1nz4|1NZ4]], [[1nz5|1NZ5]], [[1rse|1RSE]], [[1wla|1WLA]], [[1xch|1XCH]], [[1yma|1YMA]], [[1ymb|1YMB]], [[1ymc|1YMC]], [[2frf|2FRF]], [[2fri|2FRI]], [[2frj|2FRJ]], [[2frk|2FRK]], [[2in4|2IN4]], [[2v1e|2V1E]], [[2v1f|2V1F]], [[2v1g|2V1G]], [[2v1h|2V1H]], [[2v1i|2V1I]], [[2v1k|2V1K]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1j OCA], [http://www.ebi.ac.uk/pdbsum/2v1j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v1j RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF RADIATION-INDUCED METMYOGLOBIN- AQUA FERROUS MYOGLOBIN AT PH 8.7'''
'''CRYSTAL STRUCTURE OF RADIATION-INDUCED METMYOGLOBIN- AQUA FERROUS MYOGLOBIN AT PH 8.7'''
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[[Category: Gorbitz, C H.]]
[[Category: Gorbitz, C H.]]
[[Category: Hersleth, H P.]]
[[Category: Hersleth, H P.]]
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[[Category: haem]]
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[[Category: Haem]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: iron]]
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[[Category: Iron]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: monooxygenase]]
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[[Category: Monooxygenase]]
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[[Category: muscle protein]]
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[[Category: Muscle protein]]
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[[Category: oxygen activation]]
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[[Category: Oxygen activation]]
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[[Category: oxygen transport]]
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[[Category: Oxygen transport]]
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[[Category: radiation]]
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[[Category: Radiation]]
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[[Category: reaction intermediate]]
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[[Category: Reaction intermediate]]
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[[Category: transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:02:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:28 2008''
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Revision as of 15:02, 4 May 2008

Image:2v1j.gif

Template:STRUCTURE 2v1j

CRYSTAL STRUCTURE OF RADIATION-INDUCED METMYOGLOBIN- AQUA FERROUS MYOGLOBIN AT PH 8.7


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

2V1J 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 Sun May 4 18:02:22 2008

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