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pubmed-article:15070344pubmed:abstractText(4-Hydroxyphenyl)pyruvate dioxygenase (HPPD) is an unusual alpha-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 alpha-KG-dependent and the extradiol dioxygenases.lld:pubmed
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pubmed-article:15070344pubmed:dateRevised2008-1-17lld:pubmed
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pubmed-article:15070344pubmed:articleTitleCD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase: correlation between oxygen activation in the extradiol and alpha-KG-dependent dioxygenases.lld:pubmed
pubmed-article:15070344pubmed:affiliationDepartment of Chemistry, Stanford University, Stanford, California 94305, USA.lld:pubmed
pubmed-article:15070344pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15070344pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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