Abstract
Publisher Summary This chapter presents a study of hemoglobin by electron paramagnetic resonance (EPR) spectroscopy. EPR has been used in the study of the biochemistry of metalloproteins as a means of elucidating certain physical and chemical properties of the metal sites. Applications of EPR to biochemistry can be divided into two classes. The first includes those studies that give qualitative information concerning the presence of paramagnetic metal atoms and the changes that they may undergo, without consideration of quantitative information concerning the chemical physics relating to their physical environments. The second class includes those studies that yield information concerning the specific physical environments of metal atoms in metalloproteins. EPR absorption spectra are observed not only for the iron atom of hemoglobin but also for hemoglobin substituted with other paramagnetic metal atoms, as well as for free radicals attached to the protein. The cases in which EPR spectra are the most tractable for physical interpretation are those in which no crystal-field splitting is present. The chapter also describes the paramagnetic states of hemoglobin.
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