Structure and mechanism of copper, zinc superoxide dismutase.

Article Details

Citation

Copy to clipboard

Tainer JA, Getzoff ED, Richardson JS, Richardson DC

Structure and mechanism of copper, zinc superoxide dismutase.

Nature. 1983 Nov 17-23;306(5940):284-7. doi: 10.1038/306284a0.

PubMed ID

6316150 [ View in PubMed

]

Abstract

Copper, zinc superoxide dismutase (SOD) catalyses the very rapid two-step dismutation of the toxic superoxide radical (O-2) to molecular oxygen and hydrogen peroxide through the alternate reduction and oxidation of the active-site copper. We report here that after refitting and further refinement of the previous 2 A structure of SOD2, analysis of the new model and its calculated molecular surface shows an extensive surface topography of sequence-conserved residues stabilized by underlying tight packing and H-bonding. There is a single, highly complementary position for O-2 to bind to both the Cu(II) and activity-important Arg 141 with correct geometry; two water molecules form a ghost of the superoxide in this position. The geometry and molecular surface of the active site, together with biochemical data, suggest a specific model for the enzyme mechanism.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Zinc acetate	Superoxide dismutase [Cu-Zn]	Protein	Humans	Unknown	Ligand	Details