2v1e: Difference between revisions

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[[Image:2v1e.gif|left|200px]]
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{{STRUCTURE_2v1e|  PDB=2v1e  |  SCENE=  }}  
{{STRUCTURE_2v1e|  PDB=2v1e  |  SCENE=  }}  


'''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===




==Overview==
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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 (&lt;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.
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{{ABSTRACT_PUBMED_17565988}}


==About this Structure==
==About this Structure==
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==Reference==
==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://www.ncbi.nlm.nih.gov/pubmed/17565988 17565988]
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://www.ncbi.nlm.nih.gov/pubmed/17565988 17565988]
An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2., Hersleth HP, Dalhus B, Gorbitz CH, Andersson KK, J Biol Inorg Chem. 2002 Mar;7(3):299-304. Epub 2001 Oct 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11935353 11935353]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Reaction intermediate]]
[[Category: Reaction intermediate]]
[[Category: Transport]]
[[Category: Transport]]
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Revision as of 14:08, 29 July 2008

File:2v1e.png

Template:STRUCTURE 2v1e

CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8CRYSTAL STRUCTURE OF RADIATION-INDUCED MYOGLOBIN COMPOUND II- INTERMEDIATE H AT PH 6.8

Template:ABSTRACT PUBMED 17565988

About this StructureAbout this Structure

2V1E is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

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

An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2., Hersleth HP, Dalhus B, Gorbitz CH, Andersson KK, J Biol Inorg Chem. 2002 Mar;7(3):299-304. Epub 2001 Oct 11. PMID:11935353

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