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

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.

• Authors: Richard W D Welford, Joanna M Kirkpatrick, Luke A McNeill, Munish Puri, Neil J Oldham, Christopher J Schofield
• Journal: FEBS letters (FEBS Lett) Vol. 579 Issue 23 Pg. 5170-4 (Sep 26 2005) ISSN: 0014-5793 [Print] England
• PMID: 16153644 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

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

Topics

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