Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.

@article{Sugimoto2006CrystalSO,
  title={Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.},
  author={H. Sugimoto and S. Oda and T. Otsuki and T. Hino and Tadashi Yoshida and Y. Shiro},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 8},
  pages={
          2611-6
        }
}
  • H. Sugimoto, S. Oda, +3 authors Y. Shiro
  • Published 2006
  • Medicine, Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of L-Trp and incorporates both atoms of a molecule of oxygen (O2). Here we report on the x-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide. The overall structure of IDO shows two alpha-helical domains with the heme between them. A264 of the flexible loop in the heme distal side is in close proximity to the iron. A mutant analysis shows that none of the polar… Expand

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Ferryl Derivatives of Human Indoleamine 2,3-Dioxygenase*
Evidence for a ferryl intermediate in a heme-based dioxygenase
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