Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans.
Welford, Richard W.D., Kirkpatrick, Joanna M., McNeill Luke A., Puri, Munish, Oldham, Neil J. and Schofield, Christopher J. 2005, Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans., FEBS Letters, vol. 579, no. 23, pp. 5170-5174.
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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.
Field of Research
060112 Structural Biology (incl Macromolecular Modelling) 100301 Biocatalysis and Enzyme Technology 030406 Proteins and Peptides
Socio Economic Objective
970106 Expanding Knowledge in the Biological Sciences
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