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. Author manuscript; available in PMC: 2014 Sep 1.
Published in final edited form as: Nat Chem Biol. 2014 Jan 26;10(3):209–215. doi: 10.1038/nchembio.1438

Figure 1. Related mechanistic logic of the Fe/αKG halogenases and hydroxylases.

Figure 1

(a) Steps leading to formation of the H•-abstracting (halo)ferryl complexes; (b) Divergence of the mechanisms of (halo)ferryl-mediated hydroxylation (top, magenta arrows) and halogenation (bottom, green arrows); (c) structure of the native SyrB2 substrate, SyrB1-appended L-threonine (Thr-S-SyrB1). The substrate used most extensively in this study had L-2-aminobutyric acid (Aba) appended to SyrB1 (Aba-S-SyrB1), which effectively replaced the side chain hydroxyl group of Thr-S-SyrB1 by hydrogen.