Issue 4, 2005
From the journal:

Molecular BioSystems

Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate†

Luke A. McNeill,‡a   Emily Flashman,‡a   Matthew R. G. Buck,a   Kirsty S. Hewitson,a   Ian J. Clifton,a   Gunnar Jeschke,b   Timothy D. W. Claridge,a   Dominic Ehrismann,a   Neil J. Oldhama  and  Christopher J. Schofield*a  

* Corresponding authors

a The Department of Chemistry and The Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, UK

b Max Planck Institute for Polymer Research, Postfach 3148, D-55021 Mainz, Germany

Abstract

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.

Graphical abstract: Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate

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Article information

DOI
https://doi.org/10.1039/B511249B
Article type
Communication
Submitted
22 Jul 2005
Accepted
02 Aug 2005
First published
22 Aug 2005

Mol. BioSyst., 2005,1, 321-324

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Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate

L. A. McNeill, E. Flashman, M. R. G. Buck, K. S. Hewitson, I. J. Clifton, G. Jeschke, T. D. W. Claridge, D. Ehrismann, N. J. Oldham and C. J. Schofield, Mol. BioSyst., 2005, 1, 321 DOI: 10.1039/B511249B

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