Abstract
Abstract Nonheme iron halogenases require Fe(II), O 2 , α‐ketoglutarate (αKG), and a halide ion and catalyze halogenation at unactivated, aliphatic carbons on their substrates. The nonheme iron halogenase SyrB2, from Pseudomonas syringae , catalyzes chlorination of threonine during biosynthesis of the plant toxin syringomycin. The X‐ray crystal structure of SyrB2 revealed a mononuclear iron center coordinated by two histidine residues, bidentate αKG, and a chloride ion. Spectroscopic studies on the nonheme iron halogenase CytC3 from Streptomyces sp. RK95‐74 have implicated an iron(IV)‐oxo as a hydrogen atom abstracting species in a mechanism similar to the related nonheme iron dioxygenases.
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