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.
- Tainer, JA; Getzoff, ED; Richardson, JS; Richardson, DC
- November 17, 1983
Volume / Issue
- 306 / 5940
Start / End Page
- 284 - 287
International Standard Serial Number (ISSN)
Digital Object Identifier (DOI)