1vzi
From Proteopedia
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| - | [[Image:1vzi.gif|left|200px]]<br /><applet load="1vzi" size=" | + | [[Image:1vzi.gif|left|200px]]<br /><applet load="1vzi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vzi, resolution 1.15Å" /> | caption="1vzi, resolution 1.15Å" /> | ||
'''STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION'''<br /> | '''STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_baarsii Desulfovibrio baarsii] with CA, CL and FE2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] Known structural/functional Site: <scene name='pdbsite=AC1:Fe2 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1VZI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_baarsii Desulfovibrio baarsii] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=FE2:'>FE2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] Known structural/functional Site: <scene name='pdbsite=AC1:Fe2+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: redox states]] | [[Category: redox states]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:17:31 2008'' |
Revision as of 08:17, 3 February 2008
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STRUCTURE OF SUPEROXIDE REDUCTASE BOUND TO FERROCYANIDE AND ACTIVE SITE EXPANSION UPON X-RAY INDUCED PHOTOREDUCTION
Overview
Some sulfate-reducing and microaerophilic bacteria rely on the enzyme, superoxide reductase (SOR) to eliminate the toxic superoxide anion radical, (O2*-). SOR catalyses the one-electron reduction of O2*- to hydrogen, peroxide at a nonheme ferrous iron center. The structures of, Desulfoarculus baarsii SOR (mutant E47A) alone and in complex with, ferrocyanide were solved to 1.15 and 1.7 A resolution, respectively. The, latter structure, the first ever reported of a complex between, ferrocyanide and a protein, reveals that this organo-metallic compound, entirely plugs the SOR active site, coordinating the active iron through a, bent cyano bridge. The subtle structural differences between the, mixed-valence and the fully reduced SOR-ferrocyanide adducts were, investigated by taking advantage of the photoelectrons induced by X-rays., The results reveal that photo-reduction from Fe(III) to Fe(II) of the iron, center, a very rapid process under a powerful synchrotron beam, induces an, expansion of the SOR active site.
About this Structure
1VZI is a Single protein structure of sequence from Desulfovibrio baarsii with , and as ligands. Active as Superoxide reductase, with EC number 1.15.1.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction., Adam V, Royant A, Niviere V, Molina-Heredia FP, Bourgeois D, Structure. 2004 Sep;12(9):1729-40. PMID:15341736
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Categories: Desulfovibrio baarsii | Single protein | Superoxide reductase | Adam, V. | Bourgeois, D. | Molina-Heredia, F.P. | Niviere, V. | Royant, A. | CA | CL | FE2 | Dinuclear iron cluster | Electron transport | Ferrocyanide | Microspectrophotometry | Oxidoreductase | Photoreduction | Redox states
