CD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase:: Correlation between oxygen activation in the extradiol and α-KG-dependent dioxygenases
CD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase:: Correlation between oxygen activation in the extradiol and α-KG-dependent dioxygenases
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DOI：
10.1021/ja0316521
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发表时间：
2004-04-14
影响因子：
15
通讯作者：
Solomon, EI
中科院分区：
文献类型：
--
作者：
Neidig, ML;Kavana, M;Solomon, EI
(4-羟苯基)丙酮酸双加氧酶 (HPPD) 是一种不寻常的 α-酮酸依赖性非血红素铁双加氧酶，因为它将两个双氧原子合并到单个底物中，与外二醇双加氧酶类似。对催化活性亚铁位点及其与底物相互作用的 CD/MCD 研究揭示了氧活化的几何和电子结构以及机制方法，该方法将 α-KG 依赖性酶和外二醇双加氧酶联系起来。
(4-Hydroxyphenyl)pyruvate dioxygenase (HPPD) is an unusual α-keto acid-dependent non-heme iron dioxygenase as it incorporates both atoms of dioxygen into a single substrate, paralleling the extradiol dioxygenases. CD/MCD studies of the catalytically active ferrous site and its interaction with substrate reveal a geometic and electronic structure and mechanistic approach to oxygen activation which bridges those of the α-KG-dependent and the extradiol dioxygenases.