Mössbauer spectroscopy of iron-ovotransferrin: a crystal field interpretation.
Mössbauer spectra from frozen solutions of ovotransferrin were recorded in a variety of applied external magnetic fields and at various temperatures in a small applied field. The results were fitted to a simple model for the electronic structure at the iron site. This model requires admixtures of the free ion 6S and 4P states, indicating a weak cubic crystal field. Possible implications of this model regarding the binding site are discussed.
Spartalian
K
K
Department of Biochemistry, University of Vermont, Burlington 05405.
Lang
G
G
Woodworth
R C
RC
D001665:Binding Sites; D003207:Conalbumin / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D007501:Iron / Q000737:chemistry*; D008954:Models, Biological; D015204:Spectroscopy, Mossbauer; D014961:X-Ray Diffraction
D003207:Conalbumin; D007501:Iron