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Structure and mechanism of copper, zinc superoxide dismutase

Nature volume 306, pages 284–287 (1983)Cite this article

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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Author notes

  1. John A. Tainer & Elizabeth D. Getzoff

    Present address: Department of molecular Biology, Research Institue of Scripps Clinic, La Jolla, California, 92037, USA

Authors and Affiliations

  1. Department of Biochemistry, Duke Medical Center, Durham, North Carolina, 27710, USA

    John A. Tainer, Elizabeth D. Getzoff & David C. Richardson

  2. Department of Anatomy, Duke Medical Center, Durham, North Carolina, 27710, USA

    Jane S. Richardson

Authors
  1. John A. Tainer
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  2. Elizabeth D. Getzoff
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  3. Jane S. Richardson
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  4. David C. Richardson
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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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