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. Author manuscript; available in PMC: 2016 Mar 1.
Published in final edited form as: Nat Chem. 2015 Aug 3;7(9):696–702. doi: 10.1038/nchem.2306

Figure 4.

Figure 4

Representative Fe K-edge EXAFS data and Fourier transforms for CPO-I (a) and CYP119A1-I (b). Raw data are shown in black and best fits are shown in red and blue, respectively. The distances shown at the right were obtained by averaging independent measurements for CPO-I and P450-I (CYP119A1-I, CYP119A2-I, and CYP158A2*-I). These distances reveal that the Fe-S bond in P450-I is significantly shorter than in CPO-I, suggesting more electron donation from the proximal thiolate ligand to the ferryl moiety in P450. This may in part explain P450's greater propensity for C-H bond activation.