Structure and reaction mechanism in the heme dioxygenases

Igor Efimov, Jaswir Basran, Sarah J. Thackray, Sandeep Handa, Christopher G. Mowat, Emma Lloyd Raven

Research output: Contribution to journalArticle (Academic Journal)peer-review

70 Citations (Scopus)

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.(Figure Presented)

Original languageEnglish
Pages (from-to)2717-2724
Number of pages8
JournalBiochemistry
Volume50
Issue number14
DOIs
Publication statusPublished - 12 Apr 2011

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