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. Author manuscript; available in PMC: 2018 Aug 30.
Published in final edited form as: Nat Prod Rep. 2017 Aug 30;34(9):1141–1172. doi: 10.1039/c7np00034k

Fig. 9.

Fig. 9

Structure-based mechanistic studies of P450s from Streptomyces. (A) Epoxidation by PimD via the hydroperoxyferric intermediate, Cpd 0 (PDB ID: 2XBK). (B) Substrate-assisted biaryl ring coupling by CYP158A1 and CYP158A2 (PDB IDs: 2NZ5 and 2D09). The two different binding modes of the two biflaviolin substrates are shown in orange and green. (C) Intramolecular biaryl ring coupling by StaP (PDB IDs: 2Z3U). Wat644 and His250 are shown in the active site; Wat789 is liberated during the formation of Cpd I (Wang 2009). (D) Oxidative rearrangement by PntM via a carbocation intermediate (PDB IDs: 5L1O). Blue dots in each figure represent water molecules; yellow spheres depict steric hindrance.