Fig. 4: Structural origins of improved halocyclase activity in evolved FDHs.
From: Flavin-dependent halogenases catalyze enantioselective olefin halocyclization
a Effects of mutations in evolved FDHs on halocyclase activity. Mutations are listed relative to the parent in the previous row. Yields and selectivities are the average of duplicate measurements determined by LC/MS using p-bromoanisole internal standard. b Docking poses for the cationic intermediate generated upon bromination of 1 in the structure of RebH variant 3-LSR (left) and 3-LSR F111S (right). Key active site residues, including K79 and F/S111 are shown in yellow and a surface rendering of several residues is provided to illustrate the space created by F111S. The K79ε-amino-Br and Cbenzyl-Ocarboxylate distances are shown. aReaction conducted without added glutathione.
