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  • Title: Mössbauer effect in the high-potential iron-sulphur protein from Chromatium. Evidence for the state of the iron atoms.
    Author: Dickson DP, Johnson CE, Cammack R, Evans MC, Hall DO, Rao KK.
    Journal: Biochem J; 1974 Apr; 139(1):105-8. PubMed ID: 4463936.
    Abstract:
    1. The previous Mössbauer work on Chromatium high-potential iron-sulphur protein by Moss et al. (1968) and Evans et al. (1970) was extended to high applied magnetic fields. 2. Measurements of the reduced protein confirm that it is non-magnetic. 3. Spectra of the oxidized protein in applied magnetic fields clearly indicate that some iron atoms have a positive hyperfine field, which is evidence for antiferromagnetic coupling. 4. The spectra can be interpreted in terms of two types of iron atom with positive and negative hyperfine fields of 9 and 12T respectively. 5. A consideration of the chemical shifts and other evidence suggests formal valences of two Fe(3+) and two Fe(2+) atoms in the non-magnetic reduced state, and three Fe(3+) atoms and one Fe(2+) atom in the oxidized state. 6. However, no separate Fe(3+) and Fe(2+) spectra are seen, suggesting that the d electrons are not localized on particular iron atoms.
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