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Copper-zinc superoxide dismutase amino acid structure

Superoxide dismutase catalyzes the disproportionation of superoxide as 2O2 -i- 2H — O2 -I- H2O2. The Cu,Zn-superoxide dismutases are widely distributed in both plant and animal kingdoms and are found in eukaryotic cytosols. The vast majority of studies on superoxide dismutases have been made on the enzyme from bovine erythrocytes this enzyme contains 151 amino acid residues and two copper and two zinc atoms per molecule of —32,000 Da. The crystal structure of this protein has been reported (97), and the active site was shown to consist of a bimetallic (Cu,Zn) assembly (see Fig. 6). A type-2 copper center is... [Pg.326]


See other pages where Copper-zinc superoxide dismutase amino acid structure is mentioned: [Pg.33]    [Pg.151]    [Pg.281]    [Pg.130]    [Pg.11]    [Pg.200]    [Pg.197]    [Pg.3]   
See also in sourсe #XX -- [ Pg.130 , Pg.131 , Pg.132 , Pg.133 , Pg.134 , Pg.135 , Pg.136 , Pg.137 , Pg.138 , Pg.139 , Pg.140 , Pg.141 , Pg.142 , Pg.143 ]




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Acid superoxides

Copper structure

Copper superoxide dismutase

Copper-zinc

Copper-zinc superoxide dismutase structure

Dismutase

Structure amino acids

Superoxide dismutase

Superoxide dismutase structural

Zinc structure

Zinc-Superoxide Dismutase

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