Mössbauer investigation of deoxymyoglobin in a high magnetic field. Orientation of the electric field gradient and magnetic tensors.
We have examined the Mössbauer spectra of deosymyoglobin in a 6 T magnetic field in the temperature range 4.2-195 K. Spectra were fitted by the least-squares method using a phenomenological model in which the internal magnetic hyperfine field was assumed to be related to the applied field by a temperature dependent tensor õmega. The results indicate that õmega has axial symmetry and a principal axis system aligned with that of the electric field gradient (efg). The principal component of the latter is negative and lies on the symmetry axis of õmega. Our fits indicate that of efg asymmetry parameter is eta = 0.7, with no appreciable temperature dependence. Both axial and transverse components of õmega have the expected 1/T temperature dependence for T  greater than 20 K. Our experimentally determined value of eta, combined with published single crystal zero-field measurements, constrains the efg-heme relative orientation to two possibilities. In neither of these is an efg principal axis near to the heme normal.
D000818:Animals; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D009211:Myoglobin; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013057:Spectrum Analysis; D013696:Temperature
D009211:Myoglobin