Structure and reaction mechanism in the heme dioxygenases.
Structure and reaction mechanism in the heme dioxygenases.
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DOI：
10.1021/bi101732n
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发表时间：
2011-04-12
期刊：
影响因子：
2.9
通讯作者：
Raven EL
中科院分区：
文献类型：
--
作者：
Efimov I;Basran J;Thackray SJ;Handa S;Mowat CG;Raven EL
作为血红素依赖性酶家族的成员，血红素双加氧酶凭借其催化l-色氨酸氧化为N-甲酰基犬尿氨酸的能力而不同，这是色氨酸催化剂中的第一步和限速步骤。在过去的几年中，有一些重要的发展，这意味着已建立的建议，在血红素双加氧酶的反应机制需要重新评估。这篇重点综述从结构和机制的角度对这些最新进展进行了总结。它试图提出一些长期存在的问题的答案，突出尚未解决的问题，并探讨其他著名的催化血红素酶，如细胞色素P450，NO合酶和过氧化物酶的相似性和差异。
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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