Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine.

@article{Roncone2004EngineeringPA,
  title={Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine.},
  author={Raffaella Roncone and Enrico Monzani and Monica Murtas and Giuseppe Battaini and Andrea Pennati and Anna Maria Sanangelantoni and Simone Zuccotti and Martino Bolognesi and Luigi Casella},
  journal={The Biochemical journal},
  year={2004},
  volume={377 Pt 3},
  pages={717-24}
}
Atomic co-ordinates and structure factors for the T67R/S92D metMbCN mutant have been deposited with the Protein Data Bank, under accession codes 1h1x and r1h1xsf, respectively. Protein engineering and cofactor replacement have been employed as tools to introduce/modulate peroxidase activity in sperm whale Mb (myoglobin). Based on the rationale that haem peroxidase active sites are characterized by specific charged residues, the Mb haem crevice has been modified to host a haem-distalpropionate… CONTINUE READING
4 Citations
35 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 35 references

Investigations of the roles of distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin

  • S. Ozaki, M. P. Roach, T. Matsui, Y. Watanabe
  • Acc. Chem. Res
  • 2001

The hyperfine shifts in low spin iron(III) hemes: a ligand field analysis

  • I. Bertini, C. Luchinat, G. Parigi
  • Eur. J. Inorg. Chem
  • 2000

Cyanide binding

  • M. Bolognesi, C. Rosano, +5 authors P. Ascenzi
  • 1999

Similar Papers

Loading similar papers…