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==Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperature==
==Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperature==
<StructureSection load='4cvi' size='340' side='right' caption='[[4cvi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4cvi' size='340' side='right'caption='[[4cvi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cvi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CVI FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cvi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CVI FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvj|4cvj]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></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=4cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvi OCA], [https://pdbe.org/4cvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cvi RCSB], [https://www.ebi.ac.uk/pdbsum/4cvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvi ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cvi RCSB], [http://www.ebi.ac.uk/pdbsum/4cvi PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O-O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.
 
Heme enzymes. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.,Casadei CM, Gumiero A, Metcalfe CL, Murphy EJ, Basran J, Concilio MG, Teixeira SC, Schrader TE, Fielding AJ, Ostermann A, Blakeley MP, Raven EL, Moody PC Science. 2014 Jul 11;345(6193):193-7. doi: 10.1126/science.1254398. Epub 2014 Jul, 10. PMID:25013070<ref>PMID:25013070</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cvi" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cytochrome-c peroxidase]]
[[Category: Large Structures]]
[[Category: Blakeley, M P.]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Casadei, C M.]]
[[Category: Blakeley MP]]
[[Category: Gumiero, A.]]
[[Category: Casadei CM]]
[[Category: Moody, P C.E.]]
[[Category: Gumiero A]]
[[Category: Ostermann, A.]]
[[Category: Moody PCE]]
[[Category: Raven, E L.]]
[[Category: Ostermann A]]
[[Category: Electron transport]]
[[Category: Raven EL]]
[[Category: Ferric]]
[[Category: Heme]]
[[Category: Heme peroxidase]]
[[Category: Neutron]]
[[Category: Oxidoreductase]]
[[Category: Redox]]
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