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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26 Citations

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Structural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy.
TLDR
Iron K-edge X-ray absorption near edge structure (XANES) spectra were measured for oxy-forms of cytochrome P-450cam, horseradish peroxidase (HRP) and myoglobin (Mb) by using Synchrotoron Radiation of Photon Factory (Tsukuba) and indicated that the pi-character of the Fe-ligand bond increases in the order of Mb, HRP and P- 450cam. Expand
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. Expand
X-ray absorption spectroscopy of hemoglobin.
Publisher Summary This chapter discusses the results obtained by the X-Ray Absorption Spectroscopy (XAS) experimental method on the iron (Fe) site structure of hemoglobin (Hb) and the basic… Expand
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. Expand
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,… Expand
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. Expand
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… Expand
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. Expand
Changes in Fe site structure from fetal to adult hemoglobin probed by XANES.
Iron X-ray absorption near edge structure (XANES) spectra of human fetal (F) and adult (A) deoxyhemoglobin (deoxyHb) measured at the Frascati synchrotron radiation facility reveal the different… Expand
Increase of the Fe effective charge in hemoproteins during oxygenation process.
TLDR
The x-ray absorption near edge structure (XANES) spectra of hemoglobin and myoglobin have been measured at the wiggler beam line of the Frascati Synchrotron Radiation Facility and are interpreted as evidence of some increase of the positive effective charge on the iron atom upon oxygenation. Expand
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