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

被引:51
作者
Neidig, ML
Kavana, M
Moran, GR
Solomon, EI [1 ]
机构
[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA
[2] Univ Wisconsin, Dept Chem & Biochem, Milwaukee, WI 53211 USA
关键词
D O I
10.1021/ja0316521
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
(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. Copyright © 2004 American Chemical Society.
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收藏
页码:4486 / 4487
页数:2
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