Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications

Various spectroscopic methods were utilized to understand the important roles of both resting and substrate-bound forms of cysteine dioxygenase (CDO), a mononuclear non-heme Fe-dependent dioxygenase in the Fe(II) and Fe(III) states in the catalytic mechanism of the enzyme. The results provide a more complete description of several catalytically relevant species and provide support for a reaction mechanism similar to that established for many structurally related 2-His-1-carboxylate Fe(II)-dependent dioxygenases.