论文部分内容阅读
本文根据固氮酶已知的反应和络合催化原理,讨论了固氮酶的作用机理和活性中心结构;提出了由Fe_2S_2·Mo_2O_2原子簇构成的两个偶联在一起的两钼一铁三核活性中心(2 Mo—1 Fe)的看法;这两个偶联的三核活性中心也是放氢的活性中心.根据这活性中心模型,说明了各种底物分子的还原反应机理和CO只抑制分子氮、炔类、腈类、异腈类等6π-配位体型的底物分子的还原反应,而不抑制放氢反应的原因,以及ATP的作用机理和ATP/2比值与电子倒流的关系.
According to the known reaction and complexation catalytic principle of nitrogenase, the mechanism of nitrogenase activity and the active center structure were discussed. Two two-molybdenum-iron-trinuclear activity coupled with Fe_2S_2 · Mo_2O_2 clusters Center (2 Mo-1 Fe); these two coupled trinuclear active centers are also active sites for releasing hydrogen.According to this activity center model, it is demonstrated that the reduction reaction mechanism of various substrate molecules and the CO-only inhibitory molecule Nitrogen, acetylenes, nitriles, isonitriles and other 6π-ligand substrate molecules without reducing the reaction of the cause of the reaction, as well as the ATP mechanism of action and ATP / 2 ratio and the electronic backflow relationship.