Two Dimensional Infrared Spectroscopy - A New Approach to Understanding Enzyme Chemistry

二维红外光谱——理解酶化学的新方法

• 批准号: EP/D071011/1
• 负责人: Neil Hunt
• 金额: $ 107.86万
• 依托单位: University of Strathclyde
• 依托单位国家: 英国
• 项目类别: Fellowship
• 财政年份: 2006
• 资助国家: 英国
• 起止时间: 2006 至 无数据
• 项目状态: 已结题
• 来源: https://gtr.ukri.org/projects?ref=EP%2FD071011%2F1
• 关键词: Two; Dimensional; Infrared; Spectroscopy; New

We aim to observe the structural changes that occur at the active site of enzymes during their catalytic cycle. We will construct a state-of-the-art 2D-IR (two-dimensional infrared) spectrometer and ultimately develop novel visible-pump 2D-IR-probe techniques capable of following reactions in real time. These methods will be used to study the hydrogenase family of enzymes. The objective is to determine the structure of the active site and transient changes of this structure during the reactive cycle.Two-dimensional infrared (2D-IR) spectroscopy is a new technique that completely transforms the amount of information available from the infrared spectrum of a given molecule. The 2D-IR method is directly analogous to multidimensional NMR spectroscopy, which has been invaluable in the field of structural biology but which is limited by millisecond time resolution. In contrast, 2D-IR is based on nonlinear femtosecond techniques that retain all the information regarding structural dynamics lost by NMR. 2D-IR also extends ordinary (1D) methods like FTIR through the presence of cross or off-diagonal peaks indicating coupling between vibrations. These cross peaks yield previously inaccessible information on molecular structure and vibrational dynamics.

我们的目标是观察在催化循环过程中酶活性位点发生的结构变化。我们将建立一个最先进的二维红外光谱仪，并最终开发新的可见光泵浦二维红外探针技术，能够在真实的时间以下的反应。这些方法将用于研究氢化酶家族的酶。二维红外光谱（2D-IR）是一种新技术，它可以完全转换给定分子的红外光谱中的信息量。2D-IR方法直接类似于多维NMR光谱学，多维NMR光谱学在结构生物学领域中是非常宝贵的，但受到毫秒时间分辨率的限制。相比之下，2D-IR基于非线性飞秒技术，保留了NMR丢失的所有结构动力学信息。2D-IR还扩展了普通（1D）方法，如FTIR，通过存在交叉或非对角峰指示振动之间的耦合。这些交叉峰产生了以前无法获得的分子结构和振动动力学信息。

项目成果

Multiple-timescale photoreactivity of a model compound related to the active site of [FeFe]-hydrogenase.

与 [FeFe]-氢化酶活性位点相关的模型化合物的多时间尺度光反应性。

• DOI: 10.1021/ic800568k
• 发表时间: 2008
• 期刊: Inorganic chemistry
• 影响因子: 4.6
• 作者: Ridley AR

Relationship between protein structural fluctuations and rebinding dynamics in ferric haem nitrosyls.

亚硝酰亚铁血红素中蛋白质结构波动与重新结合动力学之间的关系。

• DOI: 10.1042/bj20101496
• 发表时间: 2011
• 期刊: The Biochemical journal
• 作者: Hunt NT