Abstract
Abstract Electron paramagnetic resonance spectra were recorded from single monoclinic crystals of bovine erythrocyte superoxide dismutase. Spectra were taken at various angles of rotation about the c (or blue optic) axis (Richardson, D. C., Bier, C. J., and Richardson, J. S. (1972), J. Biol. Chem. 247, 6368–6369) and about the a or b (green optic) axis of the crystal. Rotation about the blue axis (H in ab plane) yields the information that the Z components of all Cu(II) g tensors lie substantially in the ab plane, and this is confirmed by rotation about one of the green axes which yielded only very small Z component resonances (H in ac or bc plane). A maximum of eight hyperfine components were observed regardless of the orientation of the crystal. There appear to be two distinct groups of eight symmetrically degenerate (at least along their Z axes) Cu(II) ions, and the common Z axes of these two groups are off parallel by only a few degrees.
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