Oxygen bonding in human hemoglobin and its isolated subunits: a XANES study

Biochem Biophys Res Commun. 1987 Aug 31;147(1):31-8. doi: 10.1016/s0006-291x(87)80083-9.

Abstract

The X-ray absorption near edge structure (XANES) spectra of the human adult and foetal hemoglobin, of the isolated alpha and beta chains, in the oxygenated forms, and of the oxymyoglobin and carp oxyhemoglobin have been measured at the wiggler beam line of the Frascati Synchrotron radiation facility. The bonding angle of oxygen molecule at the iron site in these hemoproteins in solution, has been measured using the multiple scattering theory for data analysis.

MeSH terms

  • Animals
  • Carps
  • Fetal Hemoglobin
  • Globins
  • Humans
  • Molecular Conformation
  • Myoglobin
  • Oxygen* / metabolism
  • Oxyhemoglobins*
  • Porphyrins
  • Protein Binding
  • Protein Conformation
  • Spectrum Analysis

Substances

  • Myoglobin
  • Oxyhemoglobins
  • Porphyrins
  • Globins
  • Fetal Hemoglobin
  • Oxygen