Kinetics and mechanisms of the oxidation of myoglobin by Fe(III) and Cu(II) complexes.

@article{Hegetschweiler1987KineticsAM,
  title={Kinetics and mechanisms of the oxidation of myoglobin by Fe(III) and Cu(II) complexes.},
  author={Kaspar Hegetschweiler and Paul Saltman and Claudio Dalvit and Peter E. Wright},
  journal={Biochimica et biophysica acta},
  year={1987},
  volume={912 3},
  pages={384-97}
}
Two distinct mechanisms by which sperm whale myoglobin reduces, respectively, complexes of Fe(III) and Cu(II) and, in turn, is oxidized to metmyoglobin have been characterized. For both mechanisms, deoxymyoglobin is the active reductant. An outer sphere electron transfer, probably at the edge of the heme, is involved for Fe(III)NTA (NTA is nitrilotriacetic acid). This pathway does not involve ionic binding of the Fe(III) complex to the protein. The most reactive species of Fe(III)NTA is… CONTINUE READING