Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii.

@article{Math2007AssessingTR,
  title={Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii.},
  author={Christelle Math{\'e} and Claire Odile Weill and Tony A. Mattioli and Catherine Berthomieu and Chantal Hou{\'e}e-L{\'e}vin and Emilie Tremey and Vincent Nivi{\`e}re},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 30},
  pages={
          22207-16
        }
}
Superoxide reductase is a novel class of non-heme iron proteins that catalyzes the one-electron reduction of O(2)(.) to H(2)O(2), providing an antioxidant defense in some bacteria. Its active site consists of an unusual non-heme Fe(2+) center in a [His(4) Cys(1)] square pyramidal pentacoordination. In this class of enzyme, the cysteine axial ligand has been hypothesized to be an essential feature in the reactivity of the enzyme. Previous Fourier transform infrared spectroscopy studies on the… CONTINUE READING
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