Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase.

@article{Auclair2013StructuralCO,
  title={Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase.},
  author={Jared R Auclair and Heather R Brodkin and J Alejandro D'aquino and Gregory A. Petsko and Dagmar Ringe and Jeffrey N. Agar},
  journal={Biochemistry},
  year={2013},
  volume={52 36},
  pages={
          6145-50
        }
}
The metalloenzyme Cu/Zn-superoxide dismutase (SOD1) catalyzes the reduction of superoxide anions into molecular oxygen and hydrogen peroxide. Hydrogen peroxide can oxidize SOD1, resulting in aberrant protein conformational changes, disruption of SOD1 function, and DNA damage. Cells may have evolved mechanisms of regulation that prevent such oxidation. We observed that cysteinylation of cysteine 111 (Cys111) of SOD1 prevents oxidation by peroxide (DOI 10.1021/bi4006122 ). In this article, we… CONTINUE READING

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