Department of Chemistry, University of Leicester, Leicester, LE1 7RH, United Kingdom.
Curr Opin Chem Biol. 2012 Apr;16(1-2):60-6. doi: 10.1016/j.cbpa.2012.01.014. Epub 2012 Feb 20.
Heme iron is often used in biology for activation of oxygen. The mechanisms of oxygen activation by heme-containing monooxygenases (the cytochrome P450s) are well known, and involve formation of a Compound I species, but information on the heme-containing dioxygenase enzymes involved in tryptophan oxidation lags far behind. In this review, we gather together information emerging recently from structural, mechanistic, spectroscopic, and computational approaches on the heme dioxygenase enzymes involved in tryptophan oxidation. We explore the subtleties that differentiate various heme enzymes from each other, and use this to piece together a developing picture for oxygen activation in this particular class of heme-containing dioxygenases.
血红素铁常用于生物学中的氧气激活。含血红素单加氧酶（细胞色素 P450）的氧气激活机制众所周知，涉及形成化合物 I 物种，但涉及色氨酸氧化的含血红素双加氧酶的信息远远落后。在这篇综述中，我们汇集了最近从结构、机制、光谱和计算方法方面获得的有关参与色氨酸氧化的血红素双加氧酶的信息。我们探讨了使各种血红素酶彼此区分开来的细微差别，并利用这一点来拼凑出这一类含血红素双加氧酶中氧气激活的发展情况。
