Spectroscopic studies on two-iron ferredoxins
Spectroscopic studies on two-iron ferredoxins
复制标题
二铁铁氧还蛋白的光谱研究
DOI：
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发表时间：
1974
期刊：
影响因子：
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通讯作者：
W. Dunham
中科院分区：
文献类型：
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作者：
R. Sands;W. Dunham
磁共振技术在生物系统中的应用，使得人们可以对许多蛋白质的活性部位的性质进行详细的研究，这在以前是不可能的。在这些蛋白质中，有一类铁-硫蛋白质，它们作为电子传递蛋白质参与各种基本过程：光合作用、羟基化和固氮，仅举几例。该类中的单铁蛋白质，即红蛋白，已经通过化学、光谱和X射线晶体学技术进行了广泛研究（Lovenberg，1973），并且活性位点由结合在半胱氨酸硫配体的扭曲四面体中的单个铁原子组成。铁在氧化状态下是高自旋三价铁，在还原状态下是高自旋亚铁。这种结构如图I（α）所示。
The application of magnetic resonance techniques to biological systems has permitted a detailed study of the nature of the active sites of many proteins that had not been possible previously. Among these is the whole class of iron—sulphur proteins which have been implicated as electron transport proteins in a variety of fundamental processes: photosynthesis, hydroxylation and nitrogen fixation to name but a few. The single-iron proteins in this class, the rubredoxins, have been studied extensively by chemical, spectroscopic and X-ray crystallographic techniques (Lovenberg, 1973), and the active site is composed of a single iron atom bound in a distorted tetrahedron of cysteine sulphur ligands. The iron is high-spin ferric in the oxidized state and high-spin ferrous in the reduced state. This structure is shown in Fig. I (α).