A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.

@article{Battistoni2001AHM,
  title={A histidine-rich metal binding domain at the N terminus of Cu,Zn-superoxide dismutases from pathogenic bacteria: a novel strategy for metal chaperoning.},
  author={Andrea Battistoni and Francesca Pacello and Anna Paola Mazzetti and Christian Capo and J. Simon Kroll and Paul R Langford and Anna Sansone and Giovanna Donnarumma and Piera Valenti and Giuseppe Rotilio},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 32},
  pages={30315-25}
}
A group of Cu,Zn-superoxide dismutases from pathogenic bacteria is characterized by histidine-rich N-terminal extensions that are in a highly exposed and mobile conformation. This feature allows these proteins to be readily purified in a single step by immobilized metal affinity chromatography. The Cu,Zn-superoxide dismutases from both Haemophilus ducreyi and Haemophilus parainfluenzae display anomalous absorption spectra in the visible region due to copper binding at the N-terminal region… CONTINUE READING
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Natural His Tagging of Bacterial Cu,Zn-SODs 30325 by gest on Sptem er 7, 2017 hp://w w w .jb.org/ D

  • P. C. Wong, D. Waggoner, +6 authors J. D. Gitlin
  • May 21,
  • 2000

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