1Z03: 2-oxoquinoline 8-monooxygenase Component: Active Site Modulation By Rieske-[2fe-2s] Center Oxidation/reduction

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.
PDB ID: 1Z03Download
MMDB ID: 33249
PDB Deposition Date: 2005/3/1
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1Z03: trimeric; determined by author and by software (PISA)
Molecular Components in 1Z03
Label Count Molecule
Proteins (3 molecules)
2-oxo-1,2-dihydroquinoline 8-monooxygenase, Oxygenase Component
Molecule annotation
Chemicals (9 molecules)
* Click molecule labels to explore molecular sequence information.

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