Role of tryptophan 161 in catalysis by human manganese superoxide dismutase.

@article{Cabelli1999RoleOT,
  title={Role of tryptophan 161 in catalysis by human manganese superoxide dismutase.},
  author={Diane E. Cabelli and Yue Guan and Vincent J.-P. L{\'e}v{\^e}que and Amy S Hearn and John A. Tainer and Harry S. Nick and David N. Silverman},
  journal={Biochemistry},
  year={1999},
  volume={38 36},
  pages={11686-92}
}
Tryptophan 161 is a highly conserved residue that forms a hydrophobic side of the active site cavity of manganese superoxide dismutase (MnSOD), with its indole ring adjacent to and about 5 A from the manganese. We have made a mutant containing the conservative replacement Trp 161 --> Phe in human MnSOD (W161F MnSOD), determined its crystal structure, and measured the catalysis of the resulting mutant using pulse radiolysis to produce O(2)(*)(-). In the structure of W161F MnSOD the phenyl side… CONTINUE READING

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