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==Crystal structure of horse heart myoglobin reconstituted with manganese porphycene==
==Crystal structure of horse heart myoglobin reconstituted with manganese porphycene==
<StructureSection load='3wi8' size='340' side='right' caption='[[3wi8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3wi8' size='340' side='right'caption='[[3wi8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wi8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WI8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wi8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WI8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HNN:PORPHYCENE+CONTAINING+MN'>HNN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wi8 OCA], [http://pdbe.org/3wi8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wi8 RCSB], [http://www.ebi.ac.uk/pdbsum/3wi8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wi8 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HNN:PORPHYCENE+CONTAINING+MN'>HNN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wi8 OCA], [https://pdbe.org/3wi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wi8 RCSB], [https://www.ebi.ac.uk/pdbsum/3wi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wi8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.  
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Myoglobin reconstituted with manganese porphycene was prepared in an effort to generate a new biocatalyst and was characterized by spectroscopic techniques. The X-ray crystal structure of the reconstituted protein reveals that the artificial cofactor is located in the intrinsic heme-binding site with weak ligation by His93. Interestingly, the reconstituted protein catalyzes the H2O2-dependent hydroxylation of ethylbenzene to yield 1-phenylethanol as a single product with a turnover number of 13 at 25 degrees C and pH 8.5. Native myoglobin and other modified myoglobins do not catalyze C-H hydroxylation of alkanes. Isotope effect experiments yield KIE values of 2.4 and 6.1 for ethylbenzene and toluene, respectively. Kinetic data, log kobs versus BDE(C(sp(3))-H) for ethylbenzene, toluene, and cyclohexane, indicate a linear relationship with a negative slope. These findings clearly indicate that the reaction occurs via a rate-determining step that involves hydrogen-atom abstraction by a Mn(O) species and a subsequent rebound hydroxylation process which is similar to the reaction mechanism of cytochrome P450.
 
C(sp3)-H bond hydroxylation catalyzed by myoglobin reconstituted with manganese porphycene.,Oohora K, Kihira Y, Mizohata E, Inoue T, Hayashi T J Am Chem Soc. 2013 Nov 20;135(46):17282-5. doi: 10.1021/ja409404k. Epub 2013 Nov, 7. PMID:24191678<ref>PMID:24191678</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wi8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myoglobin|Myoglobin]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Hayashi, T]]
[[Category: Large Structures]]
[[Category: Inoue, T]]
[[Category: Hayashi T]]
[[Category: Kihira, Y]]
[[Category: Inoue T]]
[[Category: Mizohata, E]]
[[Category: Kihira Y]]
[[Category: Oohora, K]]
[[Category: Mizohata E]]
[[Category: Globin fold]]
[[Category: Oohora K]]
[[Category: Muscle]]
[[Category: Oxygen transport]]

Latest revision as of 11:45, 20 March 2024

Crystal structure of horse heart myoglobin reconstituted with manganese porphyceneCrystal structure of horse heart myoglobin reconstituted with manganese porphycene

Structural highlights

3wi8 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_HORSE Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

See Also

3wi8, resolution 2.20Å

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