嗜硫色杆菌中高电位铁硫蛋白的穆斯堡尔效应。铁原子状态的证据。
Mössbauer effect in the high-potential iron-sulphur protein from Chromatium. Evidence for the state of the iron atoms.
作者信息
Dickson D P, Johnson C E, Cammack R, Evans M C, Hall D O, Rao K K
出版信息
Biochem J. 1974 Apr;139(1):105-8. doi: 10.1042/bj1390105.
Abstract
- 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.
摘要
- 莫斯等人（1968年）和埃文斯等人（1970年）先前对嗜铬菌属高电位铁硫蛋白所做的穆斯堡尔研究扩展到了高外加磁场。2. 对还原态蛋白质的测量证实其为非磁性的。3. 外加磁场中氧化态蛋白质的光谱清楚地表明，一些铁原子具有正超精细场，这是反铁磁耦合的证据。4. 光谱可以用两种类型的铁原子来解释，其正、负超精细场分别为9T和12T。5. 对化学位移和其他证据的考虑表明，在非磁性还原态中两个铁原子为Fe(3+)，两个为Fe(2+)；在氧化态中三个铁原子为Fe(3+)，一个为Fe(2+)。6. 然而，未观察到单独的Fe(3+)和Fe(2+)光谱，这表明d电子并非定域在特定的铁原子上。
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