Site-Specific Time-Resolved Multidimensional Spectroscopy of Electron Transfer Dynamics

在这个由化学系化学结构和动力学计划A资助的项目中，密歇根大学的Kevin Kubarych教授和他的研究生们正在开发从头开始的蛋白质，以研究电子的基本运动。电子转移过程对生命至关重要，它们构成了开发新方法以获取能量并将其转化为有用形式的许多最紧迫的挑战。该项目通过一系列研讨会和会议促进光谱工具产生的研究机会。Kubarych教授的研究小组使用先进的超快激光光谱方法，使用设计的从头开始的金属酶支架实时可视化电子转移。合成和光谱相结合的方法提供了改变电子给体和受体位置的灵活性，并增加了加速桥联侧链。作为这种大分子设计策略的补充，库巴里奇实验室开发了一套基于多维光谱学的光谱工具箱。该项目还使用了一个由美国国家科学基金会资助的合作设施，即超快多维光学光谱实验室(Lumos)。流星雨正在开发中，以跟踪从飞秒到几秒的电子转移和其他光触发反应，波长范围从紫外线、可见光到红外线。这种极宽的时间和频率范围对于监测电荷在工程蛋白质中移动时结构和动力学的变化至关重要。

In this project funded by the Chemical Structure and Dynamics Program A of the Chemistry Division, Professor Kevin Kubarych of the University of Michigan and his graduate students are developing de novo ("from scratch") proteins to study the fundamental motion of electrons. Electron transfer processes are essential to life, and they underlie many of the most pressing challenges in developing new methods to harvest energy and convert it into useful forms. The project promotes research opportunities arising from spectroscopic tools such as used in the research via a series of workshops and meetings.Professor Kubarych's research group uses advanced ultrafast laser spectroscopy methods to visualize electron transfer in real time using designed de novo metalloenzyme scaffolds. The combined synthetic and spectroscopic approach offers the flexibility to change the location of the electron donor and acceptor, and to add accelerating bridging side chains. Complementing this macromolecular design strategy is a spectroscopic toolset based on multidimensional spectroscopy that has been developed in the Kubarych lab. The project also uses a collaborative NSF-funded facility, the Laboratory for Ultrafast Multidimensional Optical Spectroscopy (LUMOS). LUMOS is being developed to track electron transfer and other phototriggered reactions from femtoseconds to seconds at wavelengths ranging from the UV and visible to the infrared. This extremely broad temporal and frequency range is essential to monitor changes in structure and dynamics as the charge moves through the engineered protein.