Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases

Authors

  • Monica Mantri,

    1. Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, UK
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  • Zhihong Zhang,

    1. Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, UK
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  • Michael A. McDonough,

    1. Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, UK
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  • Christopher J. Schofield

    1. Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, UK
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C. J. Schofield, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, UK
Fax: +44 1865 275 674
Tel: +44 1865 275 625
E-mail: christopher.schofield@chem.ox.ac.uk

Abstract

Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase).

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