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.
(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.
Neidig
Michael L
ML
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Kavana
Michael
M
Moran
Graham R
GR
Solomon
Edward I
EI
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
D005296:Ferrous Compounds; D007656:Ketoglutaric Acids; D015111:4-Hydroxyphenylpyruvate Dioxygenase; D010100:Oxygen