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...