Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.
Regulation of the hypoxic response in humans is regulated by the post-translational hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(ii) cofactor and 2-oxoglutarate cosubstrate.
McNeill
Luke A
LA
The Department of Chemistry and The Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, UK.
Flashman
Emily
E
Buck
Matthew R G
MR
Hewitson
Kirsty S
KS
Clifton
Ian J
IJ
Jeschke
Gunnar
G
Claridge
Timothy D W
TD
Ehrismann
Dominic
D
Oldham
Neil J
NJ
Schofield
Christopher J
CJ
D001665:Binding Sites; D002853:Chromatography, Liquid; D005296:Ferrous Compounds / Q000737:chemistry*; D006801:Humans; D051793:Hypoxia-Inducible Factor 1 / Q000737:chemistry*; D007656:Ketoglutaric Acids / Q000737:chemistry*; D013058:Mass Spectrometry; D008958:Models, Molecular; D011393:Procollagen-Proline Dioxygenase / Q000737:chemistry*
D005296:Ferrous Compounds; D051793:Hypoxia-Inducible Factor 1; D007656:Ketoglutaric Acids; D011393:Procollagen-Proline Dioxygenase