Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.

@article{Bonin2004ActiveSG,
  title={Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.},
  author={Irena Bonin and Berta Maria Martins and Vladimir Purvanov and Susanne Fetzner and Robert Huber and Holger Dobbek},
  journal={Structure},
  year={2004},
  volume={12 8},
  pages={1425-35}
}
The soil bacterium Pseudomonas putida 86 uses quinoline as a sole source of carbon and energy. Quinoline 2-oxidoreductase (Qor) catalyzes the first metabolic step converting quinoline to 2-oxo-1,2-dihydroquinoline. Qor is a member of the molybdenum hydroxylases. The molybdenum ion is coordinated by two ene-dithiolate sulfur atoms, two oxo-ligands, and a catalytically crucial sulfido-ligand, whose position in the active site was controversial. The 1.8 A resolution crystal structure of Qor… CONTINUE READING
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