Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase.

@article{Miller2008RedoxTO,
  title={Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase.},
  author={Anne-Frances Miller},
  journal={Accounts of chemical research},
  year={2008},
  volume={41 4},
  pages={
          501-10
        }
}
Metalloenzymes catalyze some of the most demanding reactions in biochemistry, thereby enabling organisms to extract energy from redox reactions and utilize inorganic starting materials such as N 2 and CH 4. Bound metal ions bring to enzymes greater chemical versatility and reactivity than would be possible from amino acids alone. However the host proteins must control this broad reactivity, activating the metal for the intended reaction while excluding the rest of its chemical repertoire. To… CONTINUE READING
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