Bronsted Analysis of Catalytic Promicuity in Enzyme Models and Model Enzymes

大多数生物过程涉及酶的作用，酶是解释活细胞和有机体工作的中心。然而，对酶的作用还没有全面的定量了解，我们目前的理解肯定没有通过最严格的测试，即以与天然酶相媲美的速度生产催化剂。催化作用被定义为过渡态的稳定作用。我们将应用物理-有机化学、线性自由能关系中的工具来表征催化体系中的这些过渡态，这些体系不仅有一个活性，而且有几个活性(一种现象称为催化混杂)。我们希望对这些非凡的催化剂中的成键和断键过程有详细的了解，在机械化学的基础水平上追踪催化机械的演变，并了解它们过渡态的性质。

Most biological processes involve the action of enzymes, which are central for explaining the workings of living cells and organisms. However, there is no comprehensive quantitative understanding of enzyme action and our current understanding certainly fails the most severe test, that of producing catalysts with rates that rival natural enzymes. Catalysis is defined as transition state stabilisation. We will apply a tool from physical-organic chemistry, linear-free energy relationships, to characterise these transitions states in catalytic systems that have not just one, but several activities (a phenomenon called 'catalytic promiscuity'). We hope to gain detailed insight into the bond-making and -breaking processes in these remarkable catalysts, to trace the evolution of a catalytic machinery on the basic level of mechanistic chemistry and learn about the nature of their transition states.