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Electron paramagnetic resonance (EPR) spectra have been obtained on iron and copper protein complexes of human blood serum transferrin, human lactotransferrin, and conalbumins obtained from chicken, turkey, and Japanese quail egg whites. The EPR results indicate that Fe+3 and Cu+2 both bind to similar sites and that there is no magnetic interaction between the bound metal atoms. No difference between the sites binding the first and second moles of metal was detected by EPR. It is proposed that Cu+2 is bound to two tyrosyl oxygen atoms and two nitrogen atoms of the protein with square planar coordination, and that Fe+S is octahedrally coordinated to three tyrosyl oxygen atoms, two nitrogen atoms, and one bicarbonate ion.

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