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. Author manuscript; available in PMC: 2016 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2014 Sep 28;1847(1):98–108. doi: 10.1016/j.bbabio.2014.09.008

Fig. 3.

Fig. 3

Structure of the heme a3−CuB binuclear center, and Y244 and Y129, in bCcO (PDB ID: 3AG3) with respect to the positive and negative sides of the inner mitochondrial membrane [66]. The three water molecules, indicated by the red spheres are part of the water cluster near the heme a3 propionates. These three water molecules directly link the propionates of heme a3 to Tyr-129 by a H-bonding network (black dashed lines). The radical migration between Y244 and Y129 may occur through the Y244-H240-W236-Y129 network linked by H-bonds. The H-bond distances (in Å) between water molecules a, b and c and that between c and the oxygen of Y129 are indicated.