5vnu

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Current revision (14:11, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5vnu' size='340' side='right'caption='[[5vnu]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='5vnu' size='340' side='right'caption='[[5vnu]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vnu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phymc Phymc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VNU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VNU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.584&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYMC])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<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=5vnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vnu OCA], [http://pdbe.org/5vnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vnu RCSB], [http://www.ebi.ac.uk/pdbsum/5vnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vnu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vnu OCA], [https://pdbe.org/5vnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vnu RCSB], [https://www.ebi.ac.uk/pdbsum/5vnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vnu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity remains to be understood. We report that manganese and cobalt can bind to the same nonheme site and confer HCO activity in a heme-nonheme biosynthetic model in myoglobin. While the initial rates of O2 reduction by the Mn, Fe and Co derivatives are similar, the percentage of reaction active species formation are 7%, 4% and 1% and the total turnovers are 5.1 +/- 1.1, 13.4 +/- 0.7, and 82.5 +/- 2.5, respectively. These results correlate with the trends of nonheme metal-binding dissociation constants (35 microM, 22 microM and 9 microM) closely, suggesting that tighter metal binding can prevent ROS release from the active site, lessen damage to the protein, and produce higher total turnover numbers. Detailed spectroscopic, electrochemical, and computational studies found no evidence of redox cycling of manganese or cobalt in the enzymatic reactions, and suggest that structural and electronic effects related to the presence of different nonheme metals lead to observed differences in reactivity. This study of the roles of nonheme metal ions beyond the Cu and Fe found in native enzymes has provided deeper insights into nature's choice of metal ion, and reaction mechanism, and allows for finer control of the enzymatic activity, which is a basis for design of efficient catalysts for oxygen reduction reaction for fuel cells.
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Manganese and Cobalt in the Nonheme Metal-binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-inactive Mechanism.,Reed JH, Shi Y, Zhu Q, Chakraborty S, Mirts EN, Petrik ID, Bhagi-Damodaran A, Ross M, Moenne-Loccoz P, Zhang Y, Lu Y J Am Chem Soc. 2017 Aug 3. doi: 10.1021/jacs.7b05800. PMID:28768416<ref>PMID:28768416</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5vnu" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phymc]]
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[[Category: Physeter catodon]]
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[[Category: Bhagi-Damodaran, A]]
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[[Category: Bhagi-Damodaran A]]
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[[Category: Chakraborty, S]]
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[[Category: Chakraborty S]]
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[[Category: Lu, Y]]
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[[Category: Lu Y]]
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[[Category: Mirs, E N]]
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[[Category: Mirs EN]]
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[[Category: Moenne-Loccoz, P]]
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[[Category: Moenne-Loccoz P]]
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[[Category: Petrik, I D]]
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[[Category: Petrik ID]]
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[[Category: Reed, J]]
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[[Category: Reed J]]
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[[Category: Ross, M]]
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[[Category: Ross M]]
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[[Category: Shi, Y]]
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[[Category: Shi Y]]
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[[Category: Zhang, Y]]
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[[Category: Zhang Y]]
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[[Category: Zhu, Q]]
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[[Category: Zhu Q]]
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[[Category: Biosynthetic]]
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[[Category: Myoglobin]]
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[[Category: Oxygen]]
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[[Category: Oxygen transport]]
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[[Category: Reduction]]
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Current revision

Nonheme Iron Replacement in a Biosynthetic Nitric Oxide Reductase Model Performing O2 Reduction to Water: Mn-bound FeBMb

PDB ID 5vnu

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OCA

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