The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.

@article{Bocedi2013TheIO,
  title={The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.},
  author={A Alessio Bocedi and Raffaele Fabrini and Andrea Farrotti and Lorenzo Stella and Albert J Ketterman and Jens Zacho Pedersen and Nerino Allocati and Peter C. K. Lau and Stephan Grosse and Lindsay D Eltis and Antonio C Ruzzini and Thomas E Edwards and Laura Morici and Erica Del Grosso and Leonardo Guidoni and Daniele Bovi and Mario Lo Bello and Giorgio Federici and Michael W Parker and Philip G Board and Giorgio Ricci},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 34},
  pages={24936-47}
}
Glutathione transferases (GSTs) are protection enzymes capable of conjugating glutathione (GSH) to toxic compounds. During evolution an important catalytic cysteine residue involved in GSH activation was replaced by serine or, more recently, by tyrosine. The utility of these replacements represents an enigma because they yield no improvements in the affinity toward GSH or in its reactivity. Here we show that these changes better protect the cell from nitric oxide (NO) insults. In fact the… CONTINUE READING
4 Extracted Citations
69 Extracted References
Similar Papers

Referenced Papers

Publications referenced by this paper.
Showing 1-10 of 69 references

The ORCA program system

  • F. Neese
  • WIREs Comput . Mol . Sci .
  • 2012

The ORCA program system.WIREs

  • F. Neese
  • Comput. Mol. Sci
  • 2012
1 Excerpt

Similar Papers

Loading similar papers…