UV Resonance Raman Characterization of a Substrate Bound to Human Indoleamine 2,3-Dioxygenase 1.

Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. The reaction involves cleavage of the C=C bond in the Trp indole ring and insertion of two atomic oxygens from the iron-bound O into the indole 2 and 3 position. For establishment of the chemical mechanism of this unique enzymatic reaction, it is necessary to determine the conformation and electronic state of the substrate Trp bound to IDO.

Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein.

Tyrosinase (EC 1.14.18.

Activation Mechanism of the Streptomyces Tyrosinase Assisted by the Caddie Protein.

Tyrosinase (EC 1.14.18.