Structure and mechanism of copper, zinc superoxide dismutase.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Tainer, JA; Getzoff, ED; Richardson, JS; Richardson, DC

Published Date

  • November 17, 1983

Published In

Volume / Issue

  • 306 / 5940

Start / End Page

  • 284 - 287

PubMed ID

  • 6316150

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/306284a0


  • eng

Conference Location

  • England