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1kok

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[[Image:1kok.gif|left|200px]]
[[Image:1kok.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1kok |SIZE=350|CAPTION= <scene name='initialview01'>1kok</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1kok", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=HIF:FE(III)-(4-MESOPORPHYRINONE)'>HIF</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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{{STRUCTURE_1kok| PDB=1kok | SCENE= }}
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|RELATEDENTRY=[[2cyp|2CYP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kok OCA], [http://www.ebi.ac.uk/pdbsum/1kok PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kok RCSB]</span>
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}}
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'''Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)'''
'''Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)'''
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[[Category: Immoos, C E.]]
[[Category: Immoos, C E.]]
[[Category: Poulos, T L.]]
[[Category: Poulos, T L.]]
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[[Category: bifunctional catalyst]]
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[[Category: Bifunctional catalyst]]
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[[Category: cytochrome c peroxidase]]
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[[Category: Cytochrome c peroxidase]]
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[[Category: cytochrome oxidase]]
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[[Category: Cytochrome oxidase]]
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[[Category: mesoporphyrin]]
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[[Category: Mesoporphyrin]]
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[[Category: nitrite reducatse]]
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[[Category: Nitrite reducatse]]
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[[Category: proximal loop]]
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[[Category: Proximal loop]]
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[[Category: trp191 cationic radical]]
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[[Category: Trp191 cationic radical]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:25 2008''
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Revision as of 19:59, 2 May 2008

Image:1kok.gif

Template:STRUCTURE 1kok

Crystal Structure of Mesopone Cytochrome c Peroxidase (MpCcP)


Overview

The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.

About this Structure

1KOK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases., Immoos CE, Bhaskar B, Cohen MS, Barrows TP, Farmer PJ, Poulos TL, J Inorg Biochem. 2002 Sep 20;91(4):635-43. PMID:12237229 Page seeded by OCA on Fri May 2 22:59:15 2008

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