3wi8: Difference between revisions
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==Crystal structure of horse heart myoglobin reconstituted with manganese porphycene== | |||
<StructureSection load='3wi8' size='340' side='right' caption='[[3wi8]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== 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> | |||
</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> | |||
<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://www.rcsb.org/pdb/explore.do?structureId=3wi8 RCSB], [http://www.ebi.ac.uk/pdbsum/3wi8 PDBsum]</span></td></tr> | |||
</table> | |||
== 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. | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Myoglobin|Myoglobin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Hayashi, T | [[Category: Hayashi, T]] | ||
[[Category: Inoue, T | [[Category: Inoue, T]] | ||
[[Category: Kihira, Y | [[Category: Kihira, Y]] | ||
[[Category: Mizohata, E | [[Category: Mizohata, E]] | ||
[[Category: Oohora, K | [[Category: Oohora, K]] | ||
[[Category: Globin fold]] | [[Category: Globin fold]] | ||
[[Category: Muscle]] | [[Category: Muscle]] | ||
[[Category: Oxygen transport]] | [[Category: Oxygen transport]] | ||