Reactions of triethylphosphine gold(I) complexes with heme proteins: novel spin-state changes in cytochrome b562, myoglobin, and hemoglobin.

  title={Reactions of triethylphosphine gold(I) complexes with heme proteins: novel spin-state changes in cytochrome b562, myoglobin, and hemoglobin.},
  author={Martin Grootveld and Gabriel Otiko and Peter J. Sadler and Richard Cammack},
  journal={Journal of inorganic biochemistry},
  volume={27 1},
Reactions of bacterial Fe(III) cyt b562, HbO2, met Hb and met Mb with Et3PAuCl and Et3PAuNO3 (and some related complexes) have been investigated by electronic absorption and EPR and NMR spectroscopy. Except for met Hb, which denatured, the products were novel high-spin Fe(III) heme proteins. The reactions of cyt b562 and Mb were reversible. Two distinct kinetic steps were observed in the autoxidation of HbO2 and MbO2. These may involve the liberation of superoxide. Autoxidation of HbO2 occurred… 
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The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium.
  • A. Riggs
  • Medicine, Biology
    The Journal of biological chemistry
  • 1961
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The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance.
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