Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans

FEBS Lett. 2005 Sep 26;579(23):5170-4. doi: 10.1016/j.febslet.2005.08.033.

Abstract

The ferrous iron and 2-oxoglutarate (2OG) dependent oxygenases catalyse two electron oxidation reactions by coupling the oxidation of substrate to the oxidative decarboxylation of 2OG, giving succinate and carbon dioxide coproducts. The evidence available on the level of incorporation of one atom from dioxygen into succinate is inconclusive. Here, we demonstrate that five members of the 2OG oxygenase family, AlkB from Escherichia coli, anthocyanidin synthase and flavonol synthase from Arabidopsis thaliana, and prolyl hydroxylase domain enzyme 2 and factor inhibiting hypoxia-inducible factor-1 from Homo sapiens all incorporate a single oxygen atom, almost exclusively derived from dioxygen, into the succinate co-product.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Humans
  • Iron / chemistry
  • Iron / metabolism*
  • Ketoglutaric Acids / chemistry
  • Ketoglutaric Acids / metabolism*
  • Molecular Structure
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Oxygen / metabolism*
  • Oxygen Isotopes / chemistry
  • Oxygen Isotopes / metabolism
  • Oxygenases / chemistry
  • Oxygenases / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism*
  • Succinic Acid / chemistry
  • Succinic Acid / metabolism*

Substances

  • Bacterial Proteins
  • Ketoglutaric Acids
  • Oxygen Isotopes
  • Plant Proteins
  • Succinic Acid
  • Iron
  • Oxygenases
  • Oxygen