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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
