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

Rok Sekirnik; Nathan R. Rose; Jasmin Mecinović; Christopher J. Schofield

doi:10.1039/C004952B

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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

Author affiliations

* 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.

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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

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Metallomics, 2010,2, 397-399

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Metallomics

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

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