1gjn
From Proteopedia
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| - | [[Image:1gjn.gif|left|200px]]<br /><applet load="1gjn" size=" | + | [[Image:1gjn.gif|left|200px]]<br /><applet load="1gjn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gjn, resolution 1.35Å" /> | caption="1gjn, resolution 1.35Å" /> | ||
'''HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2'''<br /> | '''HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GJN 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 SO4, HEM and HYD as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1GJN 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=HYD:'>HYD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: reaction intermediate]] | [[Category: reaction intermediate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:40:26 2008'' |
Revision as of 07:40, 3 February 2008
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HYDROGEN PEROXIDE DERIVED MYOGLOBIN COMPOUND II AT PH 5.2
Overview
The biological conversions of O(2) and peroxides to water as well as, certain incorporations of oxygen atoms into small organic molecules can be, catalyzed by metal ions in different clusters or cofactors. The catalytic, cycle of these reactions passes through similar metal-based complexes in, which one oxygen- or peroxide-derived oxygen atom is coordinated to an, oxidized form of the catalytic metal center. In haem-based peroxidases or, oxygenases the ferryl (Fe(IV)O) form is important in compound I and, compound II, which are two and one oxidation equivalents higher than the, ferric (Fe(III)) form, respectively. In this study we report the 1.35 A, structure of a compound II model protein, obtained by reacting hydrogen, peroxide with ferric myoglobin at pH 5.2. The molecular geometry is, virtually unchanged compared to the ferric form, indicating that these, reactive intermediates do not undergo large structural changes. It is, further suggested that at low pH the dominating compound II resonance form, is a hydroxyl radical ferric iron rather than an oxo-ferryl form, based on, the short hydrogen bonding to the distal histidine (2.70 A) and the Fe...O, distance. The 1.92 A Fe...O distance is in agreement with an EXAFS study, of compound II in horseradish peroxidase.
About this Structure
1GJN is a Single protein structure of sequence from Equus caballus with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Feb 3 09:40:26 2008
Categories: Equus caballus | Single protein | Andersson, K.K. | Dalhus, B. | Gorbitz, C.H. | Hersleth, H.P. | HEM | HYD | SO4 | Ferryl | Haem | Heme | Hydroxy radical | Monooxygenase | Oxygen activation | Peroxidase | Reaction intermediate
