Structure and mechanism of copper, zinc superoxide dismutase

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


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Catalysis
  • Copper
  • Cyanides / metabolism
  • Models, Molecular
  • Oxidation-Reduction
  • Protein Conformation
  • Superoxide Dismutase* / metabolism
  • Superoxides / metabolism
  • Zinc


  • Cyanides
  • Superoxides
  • Copper
  • Superoxide Dismutase
  • Zinc