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lüll Structure and reaction mechanism in the heme dioxygenases Efimov I; Basran J; Thackray SJ; Handa S; Mowat CG; Raven ELBiochemistry 2011[Apr]; 50 (14): 2717-24As members of the family of heme-dependent enzymes, the heme dioxygenases are differentiated by virtue of their ability to catalyze the oxidation of l-tryptophan to N-formylkynurenine, the first and rate-limiting step in tryptophan catabolism. In the past several years, there have been a number of important developments that have meant that established proposals for the reaction mechanism in the heme dioxygenases have required reassessment. This focused review presents a summary of these recent advances, written from a structural and mechanistic perspective. It attempts to present answers to some of the long-standing questions, to highlight as yet unresolved issues, and to explore the similarities and differences of other well-known catalytic heme enzymes such as the cytochromes P450, NO synthase, and peroxidases.|Animals[MESH]|Biocatalysis[MESH]|Humans[MESH]|Indoleamine-Pyrrole 2,3,-Dioxygenase/chemistry/*metabolism[MESH]|Kynurenine/*analogs & derivatives/chemistry/metabolism[MESH]|Models, Molecular[MESH]|Molecular Structure[MESH]|Protein Structure, Tertiary[MESH]|Tryptophan Oxygenase/chemistry/*metabolism[MESH]|Tryptophan/chemistry/*metabolism[MESH] |