1vzh
From Proteopedia
(New page: 200px<br /> <applet load="1vzh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vzh, resolution 1.69Å" /> '''STRUCTURE OF SUPERO...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1VZH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | + | 1VZH 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 FE, CA and FC6 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZH OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15341736 15341736] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15341736 15341736] | ||
| - | [[Category: | + | [[Category: Desulfovibrio baarsii]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Superoxide reductase]] | ||
[[Category: Adam, V.]] | [[Category: Adam, V.]] | ||
[[Category: Bourgeois, D.]] | [[Category: Bourgeois, D.]] | ||
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[[Category: redox states]] | [[Category: redox states]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:15:08 2007'' |
Revision as of 12:10, 30 October 2007
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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 ... [(full description)]
About this Structure
1VZH is a [Single protein] structure of sequence from [Desulfovibrio baarsii] with FE, CA and FC6 as [ligands]. Active as [Superoxide reductase], with EC number [1.15.1.2]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 14:15:08 2007
Categories: Desulfovibrio baarsii | Single protein | Superoxide reductase | Adam, V. | Bourgeois, D. | Molina-Heredia, F.P. | Niviere, V. | Royant, A. | CA | FC6 | FE | Dinuclear iron cluster | Electron transport | Ferrocyanide | Microspectrophotometry | Oxidoreductase | Photoreduction | Redox states
