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  • Title: Structure and reaction mechanism in the heme dioxygenases.
    Author: Efimov I, Basran J, Thackray SJ, Handa S, Mowat CG, Raven EL.
    Journal: Biochemistry; 2011 Apr 12; 50(14):2717-24. PubMed ID: 21361337.
    Abstract:
    As 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.
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