Journal
FEBS JOURNAL
Volume 279, Issue 9, Pages 1563-1575Publisher
WILEY
DOI: 10.1111/j.1742-4658.2012.08496.x
Keywords
ACCO; auto-oxidation; ethylene; histone demethylases; hypoxia; JMJD6; oxidative fragmentation; reactive oxygen species; RNA splicing; self-hydroxylation; 2-oxoglutarate oxygenase
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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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