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={Serge Pin and Bernard Alpert and Alain Michalowicz},
  journal={FEBS Letters},
  year={1982},
  volume={147}
}
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27 Citations
Background Citations
3
Methods Citations
1
Results Citations
1

27 Citations

Structural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy.
Alteration of heme axial ligands in hemoglobin by organic solvents analyzed by CD, FTIR, and XANES techniques.
TLDR
The analysis of the iron CO stretching band shows that the ligand binding sites of alpha CO and beta CO subunits inside the alpha 2 beta 2 hemoglobin tetramer exhibit multiple conformations, suggesting that the protein affinity could be associated with a hierarchy of subtle dynamic states.
Ligand binding processes in hemoglobin. Chemical reactivity of iron studied by XANES spectroscopy.
X-ray absorption spectroscopy of hemoglobin.
Using porphyrin-amino acid pairs to model the electrochemistry of heme proteins: experimental and theoretical investigations.
TLDR
This study attempts to understand the molecular interactions that can control electrochemical reversibility in heme proteins and can be scaled up to build a heme-amino acid interaction database that may predict the electrochemical properties of any protein with a defined polypeptide sequence.
X-Ray absorption spectroscopy of iron-(II) and -(III) basket-handle porphyrins
X-Ray absorption near-edge structure and extended X-ray absorption fine structure spectroscopies have been used to characterize iron basket-handle porphyrins in various co-ordinations,…
Dioxygen Binding to Protonated Heme in the Gas Phase, an Intermediate Between Ferric and Ferrous Heme.
TLDR
A study of the UV/Vis action spectra and binding energies of heme-O2 molecules has been undertaken in the gas phase, resulting in a delocalization of the positive charge over the porphyrin cycle, such that the Fe atom bears a fractional positive charge.
X-ray absorption spectroscopic studies on iron in soybean lipoxygenase: a model for mammalian lipoxygenases
X-ray absorption spectroscopy studies are contributing both to the refinement of the geometry of metal sites already known from crystallographic studies and the elucidation of the coordination sphere…
Bonding of heme Fe(III) with dioxygen: observation and characterization of an incipient bond.
TLDR
This first observation and characterization of the ferric heme-O2 ionic complex is presented, showing the formation of an incipient Fe-O bond, confirmed by the electronic absorption spectra of the two complexes.
Changes in Fe site structure from fetal to adult hemoglobin probed by XANES.
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References

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TLDR
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Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
J. J. WEISS1 has proposed that oxyhæmoglobin is a hæmoglobin peroxide, with the iron atom in the ferric state and the oxygen molecule present as an O−2 ion, which is then taken up in the…
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