Fig. 6: Summary of active site configurations observed for D2O2-soaked, reduced, and oxidized Trp161Phe MnSOD. | Nature Communications

Fig. 6: Summary of active site configurations observed for D2O2-soaked, reduced, and oxidized Trp161Phe MnSOD.

From: Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition

Fig. 6

a Dioxygen-bound Trp161Phe MnSOD is seen in chain B. The singly-protonated dioxygen species bound to the metal ion (Fig. 2b) is probably hydroperoxyl anion as supported by our XAS measurements (Fig. 3) and DFT calculations (Fig. 4, Table 2). A D2O2 molecule is also coordinated between His30 and Tyr34 with SSHBs (Fig. 5a). b Active site of Trp161Phe MnSOD chain A was treated with D2O2, though cryocooling did not capture any dioxygen species (Fig. 5b). c Reduced resting state of Trp161Phe MnSOD (Figs. 2c, 5c). d Oxidized resting state of Trp161Phe MnSOD (Figs. 2e, 5d). All neutron structure active sites are shown in Supplementary Fig. 2. Dashed lines represent normal hydrogen bonds, and wide dashed lines are SSHBs. The portrayal of structures and bond lengths in 2D are not representative of those seen experimentally in 3D.

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