An investigation by iron K‐edge spectroscopy of the oxidation state of iron in hemoglobin and its subunits

@article{Pin1982AnIB,
  title={An investigation by iron K‐edge spectroscopy of the oxidation state of iron in hemoglobin and its subunits},
  author={S. Pin and B. Alpert and A. Michalowicz},
  journal={FEBS Letters},
  year={1982},
  volume={147}
}
Although the change in hemoglobin affinity for oxygen (the cooperative effects [1]) is known to be accompanied by some modifications in protein conformation [2], the processes which control the hemoglobin iron affinity for the ligands are still poorly understood. A variety of chemical 13-51 and spectroscopic studies [6-81 on hemoglobin have not yet attributed the formal charge of the iron bound to the oxygen molecule. Likewise, the oxidation state and degree of covalency of the iron in other… Expand
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