Issue 6, 2010
From the journal:

Metallomics

2-Oxoglutarate oxygenases are inhibited by a range of transition metals

Rok Sekirnik,a   Nathan R. Rose,a   Jasmin Mecinović†a  and  Christopher J. Schofield*a  

* Corresponding authors

a Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK
E-mail: christopher.schofield@chem.ox.ac.uk
Fax: +44 1865 285002
Tel: +44 1865 275625

Abstract

2-Oxoglutarate oxygenases are inhibited by a range of transition metals, as exemplified by studies on human histone demethylases and prolyl hydroxylase domain 2 (PHD2 or EGLN1). The biological effects associated with 2-oxoglutarate oxygenase inhibition may result from inhibition of more than one enzyme and by mechanisms in addition to simple competition with the Fe(II) cofactor.

Graphical abstract: 2-Oxoglutarate oxygenases are inhibited by a range of transition metals

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Article information

DOI
https://doi.org/10.1039/C004952B
Article type
Communication
Submitted
06 Apr 2010
Accepted
07 May 2010
First published
20 May 2010

Metallomics, 2010,2, 397-399

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