EXAFS OF NOVEL FORMS OF NITROGENASE ENZYME

我们打算进一步研究 各种酶状态的固氮酶蛋白。 MoFeS M中心 是固氮的活性位点，而FeS P-团簇提供固定过程所需的电子。 我们 我也想重现一个初步的结构EXAFS数据， 电子还原固氮酶蛋白与静息蛋白比较。 最后，我们想对CO抑制的固氮酶进行研究， 建议绑定到M中心，以了解由于 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.