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FEBS J. 2012 May;279(9):1563-75. doi: 10.1111/j.1742-4658.2012.08496.x. Epub 2012 Feb 20.

Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.

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1
Department of Chemistry and the Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford, 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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