Fig. 8: Cryo-EM density map (F-state) and modelled structure of the binuclear site in CcO. | Nature Communications

Fig. 8: Cryo-EM density map (F-state) and modelled structure of the binuclear site in CcO.

From: Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase

Fig. 8

a Structural overview of the binuclear site in the F-state. No bridging ligand is located between the iron (orange) and the copper (brown) atom. Instead, the density map may indicate the presence of an oxoferryl (cyan) at the heme and a dioxide species (green) in close proximity. b Measured distances (Å) for the modelled molecules at the active site. c Top view of the binuclear center of the F-state. d Modeling of the iron of heme a3 with a bound oxygen (oxoferryl) and without. The corresponding density map is illustrated as a white surface or mesh volumes. Illustrated map densities are filtered to equal contour levels of 1.5.

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