Figure 3.

Superimpositions of the active site of chain C in complex structures. (A) Oxy: Fdred-CAR [(3), magenta] and Oxy: FdCAR [(2’), yellow]. Only the nonheme iron (sphere), waters liganded to the iron (small sphere), iron-coordinated residues (H183, H187, and D333; stick), and CAR (stick) are shown. (B) Oxy: Fdred-CAR [(3), magenta] and OMO-O in the reduced state (PDB code 1Z02, slate) [14]. (C) Oxy: Fdred-CAR [(3), magenta] and Oxy: Fdred [(2), cyan]. (D) Oxy: FdO2 [(3’), salmon], NDO-O bound with dioxygen only (PDB code 1O7M, orange), and both oxygen and indole (PDB code 1O7N, lime) [13]. Dioxygen molecule and indole are shown as stick-and-ball and stick, respectively. (E) Oxy: FdCAR-O2 [(4), white], NDO-O bound with oxygen only (PDB code 1O7M, orange), and both oxygen and indole (PDB code 1O7N, lime) [13]. (F) Oxy: FdCAR-O2 [(4), white] and Oxy: FdO2 [(3’), salmon]. (G) Oxy: FdCAR-O2 [(4), white], Oxy: FdCAR [(2’), yellow], and Oxy: Fdred-CAR [(3), magenta]. (H) Oxy: FdCAR-O2 [(4), white], Oxy: FdCAR [(2’), yellow], and Oxy: FdO2 [(3’), salmon].

Ashikawa et al. BMC Structural Biology 2012 12:15   doi:10.1186/1472-6807-12-15
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