Please use this identifier to cite or link to this item:
Title: Structure and reaction mechanism in the heme dioxygenases.
Authors: Efimov, I
Basran, J
Thackray, SJ
Handa, S
Mowat, CG
Raven, EL
First Published: 12-Apr-2011
Citation: BIOCHEMISTRY, 2011, 50 (14), pp. 2717-2724
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.
DOI Link: 10.1021/bi101732n
eISSN: 1520-4995
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Chemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.