EXAFS OF NOVEL FORMS OF NITROGENASE ENZYME

我们打算进一步研究委员会架构的改变。 各种酶状态下的固氮酶蛋白。MoFeS M-Center 是建议的固氮活性部位，而FES P-团簇提供固定过程所需的电子。我们 我还想在一台计算机上复制初步的结构化EXAFS数据 电子还原固氮酶蛋白与静息蛋白相比。 最后，我们想对CO抑制的固氮酶进行研究，这是 建议绑定到M-Center，以了解因以下原因而发生的变化 在M中心结合。

We intend to further examine changes in the structure of the nitrogenase protein in various enzymatic states. The MoFeS M-center is the proposed active site of nitrogen fixation while the FeS P-cluster provides electrons necessary for the fixation process. We also want to reproduce preliminary structural EXAFS data on one electron reduced nitrogenase protein to compare with resting protein. Finally, we want to do studies on CO-inhibited nitrogenase, which is proposed to bind to the M-center, to gain insight on changes due to binding at the M-center.