Kinetic isotope effects and transition state analysis

动力学同位素效应和过渡态分析

• 批准号: 227511-2009
• 负责人: Berti, Paul
• 金额: $ 3.64万
• 依托单位: McMaster University
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2012
• 资助国家: 加拿大
• 起止时间: 2012-01-01 至 2013-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=514270
• 关键词: Kinetic; isotope; effects; transition; state

We study enzymatic reactions by measuring kinetic isotope effects (KIEs), which allows us to determine the structures of the transition states of reactions. A transition state is the top of the energetic barrier for reactions and it is the structure which enzymes stabilize by binding tightly, thereby accelerating (catalyzing) reactions.

我们通过测量动力学同位素效应（KIEs）来研究酶促反应，这使我们能够确定反应过渡态的结构。过渡态是反应能垒的顶端，它是酶通过紧密结合来稳定的结构，从而加速（催化）反应。