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. Author manuscript; available in PMC: 2020 Oct 17.
Published in final edited form as: J Phys Chem B. 2019 Oct 3;123(41):8662–8674. doi: 10.1021/acs.jpcb.9b07228

Figure 1.

Figure 1.

a) Rate-limiting PCET reaction catalyzed by an FeIII(OH) cofactor of SLO. b) Ground state active site structure of SLO with bound linoleic acid substrate (blue), from QM/MM calculations (ref.69). Flanking side chains L754, I553, and L546 (in gray) have been the subject of various mutational studies. c) HDX-MS identified protein network connecting the surface loop and active site in SLO. Residues L546, I552, I553, S749, S750, and Y317 (shown in pink spheres) line this network (ref. 18).