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The 2-oxoglutarate (2OG)-dependent oxidases and oxygenases represent the largest family of non-haem iron enzymes.1  They employ 2OG as a cosubstrate to carry out a variety of metabolic transformations, many of which involve the cleavage of a substrate C–H bond. A consensus mechanism has emerged for 2OG-dependent enzymes leading to the formation of an Fe(iv)O species2  that is capable of a wide array of substrate oxidations, including hydroxylation, halogenation, desaturation, electrophilic aromatic substitution and epoxidation.3  Mechanistic studies, particularly by the Bollinger/Krebs group (see Chapter 3),3  have led to the proposed catalytic cycle shown in Figure... 

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