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. 2010 Apr 12;107(17):7740–7745. doi: 10.1073/pnas.0910410107

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Fig. 2. — Conformational change of helix X which occurs upon ligand bindings to . (A) Atomic models of the segment of helix X from Val380 to Met383 including hemes a and a₃. The models show the structures of the fully reduced (blue), the fully reduced CO-bound (yellow), and the fully oxidized (red) forms. The dotted surfaces denote cavities detectable in different oxidation and ligand-binding states near the two helix turns, shown with the same colors as used for the atomic models. The cavities are calculated with a probe radius of 1.3 Å. The green dotted line shows the location of the water channel in this region. (B) Schematic representations of the conformational changes induced by oxidation and ligand-binding states. (Left) the fully oxidized forms, (Center) the fully reduced CO- and NO-bound forms and (Right) the fully reduced ligand-free and CN^--bound forms. The red and blue spheres represent the positions of the fixed water molecules, the locations of which are dependent upon the oxidation state of heme a. The black spheres represent the positions of the fixed water molecules independently of the oxidation states of the metal sites.

Inline graphic — Conformational change of helix X which occurs upon ligand bindings to . (A) Atomic models of the segment of helix X from Val380 to Met383 including hemes a and a₃. The models show the structures of the fully reduced (blue), the fully reduced CO-bound (yellow), and the fully oxidized (red) forms. The dotted surfaces denote cavities detectable in different oxidation and ligand-binding states near the two helix turns, shown with the same colors as used for the atomic models. The cavities are calculated with a probe radius of 1.3 Å. The green dotted line shows the location of the water channel in this region. (B) Schematic representations of the conformational changes induced by oxidation and ligand-binding states. (Left) the fully oxidized forms, (Center) the fully reduced CO- and NO-bound forms and (Right) the fully reduced ligand-free and CN^--bound forms. The red and blue spheres represent the positions of the fixed water molecules, the locations of which are dependent upon the oxidation state of heme a. The black spheres represent the positions of the fixed water molecules independently of the oxidation states of the metal sites.