4tyx: Difference between revisions
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==Structure of aquoferric sperm whale myoglobin L29H/F33Y/F43H/S92A mutant== | |||
<StructureSection load='4tyx' size='340' side='right'caption='[[4tyx]], [[Resolution|resolution]] 1.64Å' 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]] 1.64Å</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®/PubMed®, 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]] | |||
