Differences in the dynamics of oxidized and reduced cytochrome c measured by Mossbauer spectroscopy
Differences in the dynamics of oxidized and reduced cytochrome c measured by Mossbauer spectroscopy
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DOI：
10.1007/s007750050187
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发表时间：
1997-12-01
影响因子：
3
通讯作者：
Parak, FG
中科院分区：
文献类型：
--
作者：
Frolov, EN;Gvosdev, R;Parak, FG
通过穆斯堡尔谱研究了还原和氧化细胞色素 c 中铁原子均方位移的温度依赖性。由与铁的耦合模式标记的蛋白质的灵活性在还原时会减弱。灵活性的差异足以解释氧化形式和还原形式之间物理化学性质的差异。
The temperature dependence of the mean square displacement of the iron atom in reduced and oxidized cytochrome c has been studied by Mossbauer spectroscopy. The flexibility of the protein, labeled by the modes coupling to the iron, is diminished upon reduction. The differences in flexibility are sufficient to explain the differences in physicochemical properties between the oxidized and the reduced forms.