Abstract
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 principles of the X-ray absorption spectroscopic method. X-Ray absorption spectroscopy of Hb has provided an experimental method for probing the Fe site structural configurations in solution. The spectral features in the XAS spectra are determined by the scattering of the photoelectrons, emitted by the absorbing Fe ion of Hb and returned to the Fe site by the neighboring atoms within a sphere of about 5 A°. Therefore, the XAS method is a direct probe of atomic distribution via electron diffraction. It probes the spatial distribution of the atoms of the heme, the proximal histidine, and the ligand. The absorption spectrum beyond 5 electron volt (eV) from the edge is because of transitions to high-energy states in the continuum which can be described as due to the scattering of the high-energy photoelectrons excited in the continuum from the neighboring atoms.
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