Abstract
We have used FIR magnetic resonance as a direct probe of the low lying electronic states of the high spin (S=2) ferrous ion in deoxyhemoglobin and deoxymyoglobin. In a variety of helium temperature experiments using different samples and different buffers, we have detected a broad absorption band at 3.5 cm−1 that is sensitive to the application of a magnetic field. This band is not observed in samples of oxy-or carbonmonoxy-hemoglobin. The integrated area of the absorption band agrees (via a Kramers–Kronig relation) with the measured values of the static susceptibility of deoxyhemoglobin at 1.2 °K. The large linewidth (3.5 cm−1) of the observed band is thought to reflect the large number of conformational substates associated with slightly different structures of the protein.
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