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 copper1. We report here that after refitting and further refinement of the previous 2 Å 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.
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Tainer, J., Getzoff, E., Richardson, J. et al. Structure and mechanism of copper, zinc superoxide dismutase. Nature 306, 284–287 (1983). https://doi.org/10.1038/306284a0
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DOI: https://doi.org/10.1038/306284a0
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