TRAINING IN USE OF DMX ELECTRONICS & NMR

红蛋白代表最简单的铁硫蛋白， 因为它们含有由硫原子连接的单个铁离子， 四个半胱氨酸残基的包围笼。 而红氧还蛋白 来自噬油假单胞菌的蛋白质已经被证明参与了 烷烃的羟基化作用，红氧还蛋白的生物学功能 巴氏梭菌，这是本研究的重点， 还有待发现。 由于他们的协调环境， Rubredoxins对NMR活性核表现出大的NMR化学位移 由于与未成对电子的超精细耦合， 在复杂的。 这些大的变化给了一个独特的insite进入 协调环境的电子结构。 这 信息与高级混合密度结合使用 函数计算来达到我们理解 协调环境的电子结构 铁硫蛋白

Rubredoxins represent the simplest type of iron-sulfur proteins, in that they contain a single iron ion ligated by sulfur atoms from a surrounding cage of four cysteine residues. Whereas the rubredoxin from Pseudomonas oleovorans has been shown to be involved in the hydroxylation of alkanes, the biological function of the rubredoxin from Clostridium pasteurianum, which is the focus of this study, remains to be discovered. Because of their coordination environment, rubredoxins exhibit large NMR chemical shifts for NMR-active nuclei near the iron-center due to hyperfine coupling to unpaired electrons in the complex. These large shifts give a unique insite into the electronic structure of the coordination environment. This information is used in conjunction with high-level hybrid density functional calculations to achieve our ultimate goal of understanding the electronic structure of the coordination environment of iron-sulfur proteins.