View source for 4tyx


==Structure of aquoferric sperm whale myoglobin L29H/F33Y/F43H/S92A mutant==
<StructureSection load='4tyx' size='340' side='right'caption='[[4tyx]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tyx]] 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=4TYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TYX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
<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></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=4tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tyx OCA], [https://pdbe.org/4tyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tyx RCSB], [https://www.ebi.ac.uk/pdbsum/4tyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tyx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c Oxidase (CcO) is known to catalyze the reduction of O2 to H2O efficiently with a much lower overpotential than almost all other O2 reduction catalysts. However, the methods by which the enzyme fine-tunes the reduction potential (E degrees ) of its active site and its influence on the O2 reduction activity are not well understood. In this work, we report systematic tuning of the heme E degrees in a functional model of CcO in myoglobin containing three histidines and one tyrosine in the distal pocket of heme. By removing H-bonding interactions between Ser92, and the proximal His ligand through Ser92Ala mutation, we have increased the heme E degrees from 95 +/- 2 mV to 123 +/- 3 mV . Additionally, replacing the native heme b in the protein with heme a analogs, diacetyl, monoformyl and diformyl heme, resulted in an E degrees value of 175 +/- 5 mV, 210 +/- 6 mV and 320 +/- 10 mV, respectively. Interestingly, a strong enhancement of the O2 reduction activity was observed with increasing heme E degrees . The methods of tuning the heme E degrees through a combination of secondary sphere mutations and heme substitutions can be applied to tune E degrees of other heme proteins, allowing for comprehensive investigations of the relationship between E degrees and enzymatic activity.

Systematic Tuning of Heme Redox Potentials and its Effects on O Reduction Rates in a Designed Oxidase in Myoglobin.,Bhagi-Damodaran A, Petrik ID, Marshall NM, Robinson H, Lu Y J Am Chem Soc. 2014 Jul 30. PMID:25076049<ref>PMID:25076049</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4tyx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Bhagi-Damodaran A]]
[[Category: Lu Y]]
[[Category: Petrik ID]]
[[Category: Robinson H]]