Role of Oxygen Motion in the Temperature Dependence of ΔE in Oxyhemoglobin and Model Compounds
Hemoglobin is the most intensively studied of the biological macromolecules; it has served and continues to serve as the proving ground for techniques and ideas which are leading toward a detailed understanding of life processes in general. In view of the fact that reversible combination with oxygen is the primary function of this molecule, it is a sobering thought to realize that the nature of the attachment of the oxygen is only poorly understood. There is no general agreement on the disposition of bonding electrons. General agreement as to the geometric arrangement of the oxygen and the iron atom of the binding site has been achieved only recently. The oxygenated form of hemoglobin, having spin-paired electrons, is EPR-silent. Fortunately, however, a site-specific probe is available in the form of 57Fe Mössbauer spectroscopy.
KeywordsModel Compound Quadrupole Splitting Electric Field Gradient Iron Nucleus Mossbauer Spectrum
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