1z01
From Proteopedia
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2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction
Overview
2-Oxoquinoline 8-monooxygenase is a Rieske non-heme iron oxygenase that catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline in the soil bacterium Pseudomonas putida 86. The crystal structure of the oxygenase component of 2-oxoquinoline 8-monooxygenase shows a ring-shaped, C3-symmetric arrangement in which the mononuclear Fe(II) ion active site of one monomer is at a distance of 13 A from the Rieske-[2Fe-2S] center of a second monomer. Structural analyses of oxidized, reduced, and substrate bound states reveal the molecular bases for a new function of Fe-S clusters. Reduction of the Rieske center modulates the mononuclear Fe through a chain of conformational changes across the subunit interface, resulting in the displacement of Fe and its histidine ligand away from the substrate binding site. This creates an additional coordination site at the mononuclear Fe(II) ion and can open a pathway for dioxygen to bind in the substrate-containing active site.
About this Structure
1Z01 is a Single protein structure of sequence from Pseudomonas putida with and as ligands. Active as 2-hydroxyquinoline 8-monooxygenase, with EC number 1.14.13.61 Full crystallographic information is available from OCA.
Reference
2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction., Martins BM, Svetlitchnaia T, Dobbek H, Structure. 2005 May;13(5):817-24. PMID:15893671
Page seeded by OCA on Thu Feb 21 16:10:51 2008
