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]] 2.20&Aring;' scene=''>
+<StructureSection load='3wi8' size='340' side='right'caption='[[3wi8]], [[Resolution|resolution]] 2.20&Aring;' 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>
+<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://www.rcsb.org/pdb/explore.do?structureId=3wi8 RCSB], [http://www.ebi.ac.uk/pdbsum/3wi8 PDBsum]</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>
 == 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>
 ==See Also==
-*[[Myoglobin|Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[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]]