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}
}
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.
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.
...
...

References

SHOWING 1-10 OF 21 REFERENCES
Structure-function relations in hemoglobin as determined by x-ray absorption spectroscopy.
TLDR
Conclusions concerning the structure around the iron atom in oxy- and carbonmonoxyhemoglobin have been obtained by fluorescent x-ray absorption studies and it is shown that the strain energy at the iron is less than or equal to 4 X 10(-3) eV.
X-ray absorption edge studies on oxidized and reduced cytochrome c oxidase.
  • V. Hu, S. Chan, G. Brown
  • Physics, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1977
TLDR
The x-ray absorption edge spectra of the Cu and Fe-centers in oxidized and reduced cytochrome c oxidase have been obtained using synchrotron radiation from the SPEAR storage ring at the Stanford Linear Accelerator Center and indicate that one of the two coopers in the oxidized protein is in the +1 oxidation state.
The iron–oxygen bond in human oxyhaemoglobin
TLDR
The stereochemistry of the haem–oxygen complex in human oxyHb, as determined by single-crystal X-ray analysis, is reported, suggesting that the hydrogen bond is weaker than in oxyMb7.
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
  • J. Weiss
  • Biology, Computer Science
    Nature
  • 1964
TLDR
The facts suggest that the conversion of hæmoglobin into oxyhâmoglobin is associated with a more profound electronic rearrangement.
Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery
The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect
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
Structure of horse carbonmonoxyhaemoglobin.
...
...