This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1vzi
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Some sulfate-reducing and microaerophilic bacteria rely on the enzyme | + | 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== | ==About this Structure== | ||
| Line 16: | Line 16: | ||
[[Category: Adam, V.]] | [[Category: Adam, V.]] | ||
[[Category: Bourgeois, D.]] | [[Category: Bourgeois, D.]] | ||
| - | [[Category: Molina-Heredia, F | + | [[Category: Molina-Heredia, F P.]] |
[[Category: Niviere, V.]] | [[Category: Niviere, V.]] | ||
[[Category: Royant, A.]] | [[Category: Royant, A.]] | ||
| Line 30: | Line 30: | ||
[[Category: redox states]] | [[Category: redox states]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:55 2008'' |
Revision as of 13:38, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 15:38:55 2008
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
