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Incorporation of oxygen into the succinate co‐product of iron(II) and 2‐oxoglutarate dependent oxygenases from bacteria, plants and humans
Author(s) -
Welford Richard W.D.,
Kirkpatrick Joanna.M.,
McNeill Luke A.,
Puri Munish,
Oldham Neil J.,
Schofield Christopher J.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.08.033
Subject(s) - oxygenase , chemistry , decarboxylation , dioxygenase , escherichia coli , biochemistry , ferrous , enzyme , stereochemistry , catalysis , organic chemistry , gene
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.