Hydrogen Tunneling in Enzyme Reactions

酶反应中的氢隧道

• 批准号: 8911632
• 负责人: Judith Klinman
• 金额: $ 22.18万
• 依托单位: University of California-Berkeley
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1990
• 资助国家: 美国
• 起止时间: 1990-04-15 至 1995-03-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8911632&HistoricalAwards=false
• 关键词: Hydrogen; Tunneling; Enzyme; Reactions

Recent studies from this laboratory have established that hydrogen tunneling occurs in the yeast alcohol dehydrogenase and bovine serum amine oxidase reactions. These initial findings suggest that room temperature tunneling may be fundamental feature of enzyme catatlyzed hydrogen transfer reactions. Investigation will be extended in order to: (i) Determine the generality of hydrogen tunneling in enzyme catalyzed H:, H. and H+ reactions, thereby establishing a data base for such behavior; (ii) Characterize the parameters which are likely to control the probability of tunneling, in particular the roles of reaction driving force, E.S binding interactions and protein motion; and (iii) Initiate computational work, with the goal of discriminating among possible models for nuclear tunneling at enzyme active sites. Ultimately, such studies are expected to provide insight into the shape of reaction coordinates at enzyme active sites. Over the past few years the role of quantum mechanical effects in enzyme reactions have gained importance. Although the area of electron tunneling has been the focus of extensive on going investigatrions the phenomenon of hydrogen tunneling in biology has received relatively little attention. It is a particular promising area to pursue to find answer too many features of enzyme catalysis.

该实验室最近的研究表明， 氢隧穿发生在酵母醇脱氢酶中， 牛血清胺氧化酶反应。 这些初步发现 表明室温隧穿可能是基本的 酶催化氢转移反应的特征。 将扩大调查范围，以便： (i)确定酶中氢隧穿的普遍性 催化H：、H.和H+反应，从而建立数据 这种行为的基础; (ii)表征可能控制 隧穿的概率，特别是反应的作用 驱动力、E.S结合相互作用和蛋白质运动;以及 (iii)开始计算工作，目标是 区分核隧穿的可能模型. 酶活性位点 最终，这些研究预计将 提供了深入了解酶的反应坐标的形状 活性位点。 在过去的几年里，量子力学效应在 酶反应已经变得重要。 虽然面积 电子隧穿一直是人们广泛关注的焦点 生物学中的氢隧穿现象 受到的关注相对较少。 一个特别 有前途的领域追求找到答案太多的特点 酶催化