Fig. 5: Comparison of Tyr34Phe MnSOD active site configurations to wildtype and Trp161Phe. | Nature Communications

Fig. 5: Comparison of Tyr34Phe MnSOD active site configurations to wildtype and Trp161Phe.

From: The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase

Fig. 5

a Wildtype oxidized resting state from chain B of PDB ID 7KKS13. b Tyr34Phe oxidized resting state from chain A (present study, Figs. 3e, 4e). c Wildtype reduced resting state from chain B of PDB ID 7KKW13. d Tyr34Phe reduced resting state from chain A (present study, Figs. 3c, 4c). e The product-inhibited complex of Trp161Phe, consisting of a HO2- molecule bound to a reduced active site. From chain B of PDB ID 8VHW63. f The product-inhibited complex of Tyr34Phe, consisting of a HO2- molecule bound to a reduced active site. From chain A of the present study (Figs. 3a, b, 4a). Dashed lines represent normal hydrogen bonds (> 1.8 Å), wide-dashed represent SSHBs (hydrogen bonds < 1.8 Å), and round-dotted lines represent a shared proton. The portrayal of hydrogen bond lengths in 2D are not representative of those seen experimentally in 3D.

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