Changing the metal binding specificity of superoxide dismutase from Thermus thermophilus HB-27 by a single mutation.

@article{Wang2009ChangingTM,
  title={Changing the metal binding specificity of superoxide dismutase from Thermus thermophilus HB-27 by a single mutation.},
  author={Tianwen David Wang and Aidong Qiu and Fanguo Meng and Haimeng Zhou},
  journal={Molecular biotechnology},
  year={2009},
  volume={42 2},
  pages={146-53}
}
Metal binding of superoxide dismutase from Thermus thermophilus HB27 was analyzed by comparing the related structures and sequences from different origins. Mutants (Ile166Leu, Asp167Glu, and Ile166Leu-Asp167Glu) were prepared and characterized. The mutants Asp167Glu and Ile166Leu-Asp167Glu changed their binding specificities from manganese to iron, which were manifested by the differences in color of the enzyme solutions and by flame atomic absorption analysis. Specific activities of the three… CONTINUE READING

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The genome sequence of the extreme thermophile Thermus thermophilus

Nature Biotechnology • 2004
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