1Z01

2-Oxoquinoline 8-Monooxygenase Component: Active site Modulation by Rieske-[2fe-2S] Center Oxidation/Reduction

Summary for 1Z01

• Entry DOI: 10.2210/pdb1z01/pdb
• Related: 1Z02 1Z03
• Descriptor: 2-oxo-1,2-dihydroquinoline 8-monooxygenase, oxygenase component, FE (III) ION, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• Functional Keywords: monooxygenase, rieske center, oxygen binding/activation, substrate bound complex, oxidoreductase
• Biological source: Pseudomonas putida
• Total number of polymer chains: 6
• Total formula weight: 309164.89

Authors

Martins, B.M.,Svetlitchnaia, T.,Dobbek, H. (deposition date: 2005-03-01, release date: 2005-05-24, Last modification date: 2024-03-13)

Primary citation

Martins, B.M.,Svetlitchnaia, T.,Dobbek, H.
2-Oxoquinoline 8-Monooxygenase Oxygenase Component: Active Site Modulation by Rieske-[2Fe-2S] Center Oxidation/Reduction
Structure, 13:817-824, 2005

PubMed Abstract: 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.

PubMed: 15893671
DOI: 10.1016/j.str.2005.03.008

Experimental method

X-RAY DIFFRACTION (1.8 Å)