Structural analysis of peroxide-soaked MnSOD crystals reveals side-on binding of peroxide to active-site manganese.

@article{Porta2010StructuralAO,
  title={Structural analysis of peroxide-soaked MnSOD crystals reveals side-on binding of peroxide to active-site manganese.},
  author={Jason Porta and Ardeschir Vahedi-Faridi and Gloria E O Borgstahl},
  journal={Journal of molecular biology},
  year={2010},
  volume={399 3},
  pages={377-84}
}
The superoxide dismutase (SOD) enzymes are important antioxidant agents that protect cells from reactive oxygen species. The SOD family is responsible for catalyzing the disproportionation of superoxide radical to oxygen and hydrogen peroxide. Manganese- and iron-containing SOD exhibit product inhibition whereas Cu/ZnSOD does not. Here, we report the crystal structure of Escherichia coli MnSOD with hydrogen peroxide cryotrapped in the active site. Crystallographic refinement to 1.55 A and close… CONTINUE READING
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