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
- 20 March 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (14), 4486-4487
- https://doi.org/10.1021/ja0316521
Abstract
(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.Keywords
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