4cvi: Difference between revisions
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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]] 2.10Å' scene=''> | <StructureSection load='4cvi' size='340' side='right' caption='[[4cvi]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvj|4cvj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvj|4cvj]]</td></tr> | ||
<tr id='activity'><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='activity'><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'>[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> | <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=4cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvi OCA], [http://pdbe.org/4cvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cvi RCSB], [http://www.ebi.ac.uk/pdbsum/4cvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cvi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome c peroxidase|Cytochrome c peroxidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:30, 6 August 2016
Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperatureNeutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperature
Structural highlights
Function[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMedHeme 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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