title: CD 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.
abstract: (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.
authors.affiliation: Department of Chemistry, Stanford University, Stanford, California 94305, USA.
authors.forename: Michael L
authors.initials: ML
authors.lastname: Neidig
authors.forename: Michael
authors.initials: M
authors.lastname: Kavana
authors.forename: Graham R
authors.initials: GR
authors.lastname: Moran
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
mesh_terms: D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002942:Circular Dichroism / Q000379:methods; D005296:Ferrous Compounds / Q000737:chemistry* / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism
chemical_list: D005296:Ferrous Compounds; D007656:Ketoglutaric Acids; D015111:4-Hydroxyphenylpyruvate Dioxygenase; D010100:Oxygen