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

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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.