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Metal—ligand bonds superoxide dismutase

The chelate effect in proteins is also important, since the three-dimensional (3-D) structure of the protein can impose particular coordination geometry on the metal ion. This determines the ligands available for coordination, their stereochemistry and the local environment, through local hydrophobicity/hydrophilicity, hydrogen bonding by nearby residues with bound and non-bound residues in the metal ion s coordination sphere, etc. A good example is illustrated by the Zn2+-binding site of Cu/Zn superoxide dismutase, which has an affinity for Zn2+, such that the non-metallated protein can extract Zn2+ from solution into the site and can displace Cu2+ from the Zn2+ site when the di-Cu2+ protein is treated with excess Zn2+. [Pg.18]


See other pages where Metal—ligand bonds superoxide dismutase is mentioned: [Pg.200]    [Pg.202]    [Pg.32]    [Pg.299]    [Pg.117]    [Pg.197]    [Pg.5510]    [Pg.614]    [Pg.267]    [Pg.5509]    [Pg.198]    [Pg.104]    [Pg.545]    [Pg.235]   
See also in sourсe #XX -- [ Pg.168 ]




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Dismutase

Ligands metal-ligand bonds

Ligands superoxide dismutase

Metal superoxides

Metal-ligand bonding

Metal-ligand bonds

Metals metal-ligand bond

Superoxide dismutase

Superoxide dismutase liganding

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