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

J Am Chem Soc. 2004 Apr 14;126(14):4486-7. doi: 10.1021/ja0316521.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 4-Hydroxyphenylpyruvate Dioxygenase / chemistry*
  • 4-Hydroxyphenylpyruvate Dioxygenase / metabolism
  • Binding Sites
  • Circular Dichroism / methods
  • Ferrous Compounds / chemistry*
  • Ferrous Compounds / metabolism
  • Ketoglutaric Acids / chemistry*
  • Ketoglutaric Acids / metabolism
  • Oxygen / chemistry*
  • Oxygen / metabolism

Substances

  • Ferrous Compounds
  • Ketoglutaric Acids
  • 4-Hydroxyphenylpyruvate Dioxygenase
  • Oxygen