1Z03

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

1Z03 の概要

• エントリーDOI: 10.2210/pdb1z03/pdb
• 分子名称: 2-oxo-1,2-dihydroquinoline 8-monooxygenase, oxygenase component, FE (III) ION, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total)
• 機能のキーワード: monooxygenase, rieske center, oxygen binding/activation, substrate bound complex, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 310035.83

構造登録者

Martins, B.M.,Svetlitchnaia, T.,Dobbek, H. (登録日: 2005-03-01, 公開日: 2005-05-24, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)