3re8

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3re8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RE8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3re8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RE8 FirstGlance]. <br>
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</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>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rgp|3rgp]], [[3rgs|3rgs]]</div></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></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catalase Catalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=3re8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3re8 OCA], [https://pdbe.org/3re8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3re8 RCSB], [https://www.ebi.ac.uk/pdbsum/3re8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3re8 ProSAT]</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=3re8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3re8 OCA], [https://pdbe.org/3re8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3re8 RCSB], [https://www.ebi.ac.uk/pdbsum/3re8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3re8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CATA_BOVIN CATA_BOVIN]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.
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[https://www.uniprot.org/uniprot/CATA_BOVIN CATA_BOVIN] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We present the structures of bovine catalase in its native form and complexed with ammonia and nitric oxide, obtained by X-ray crystallography. Using the NO generator 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, we were able to generate sufficiently high NO concentrations within the catalase crystals that substantial occupation was observed despite a high dissociation rate. Nitric oxide seems to be slightly bent from the heme normal that may indicate some iron(II) character in the formally ferric catalase. Microspectrophotometric investigations inline with the synchrotron X-ray beam reveal photoreduction of the central heme iron. In the cases of the native and ammonia-complexed catalase, reduction is accompanied by a relaxation phase. This is likely not the case for the catalase NO complex. The kinetics of binding of NO to catalase were investigated using NO photolyzed from N,N'-bis(carboxymethyl)-N,N'-dinitroso-p-phenylenediamine using an assay that combines catalase with myoglobin binding kinetics. The off rate is 1.5 s(-1). Implications for catalase function are discussed.
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Interaction of Nitric Oxide with Catalase: Structural and Kinetic Analysis.,Purwar N, McGarry JM, Kostera J, Pacheco AA, Schmidt M Biochemistry. 2011 May 6. PMID:21524057<ref>PMID:21524057</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 3re8" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Catalase 3D structures|Catalase 3D structures]]
*[[Catalase 3D structures|Catalase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Catalase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Purwar, N]]
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[[Category: Purwar N]]
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[[Category: Schmidt, M]]
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[[Category: Schmidt M]]
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[[Category: Disproportionation of the hydrogen peroxide]]
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[[Category: Oxidoreducatase]]
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[[Category: Oxidoreductase]]
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[[Category: The 5-coordinated heme protein]]
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Current revision

Structural and Kinetic Analysis of the Beef liver Catalase interacting with Nitric Oxide

PDB ID 3re8

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