Abstract
The Mössbauer spectra of horse heart ferri- and ferrocytochrome c were obtained at room temperature using lyophilized powders. The Mössbauer data indicate that the iron in both lyophilized samples is in a low-spin state. The high quadrupole splittings suggest that the iron atom is in an asymmetric ligand field. Upon reduction the asymmetry increases, suggesting a change in the bonding between the protein moieties and the iron atom.
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Selected References
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