Supporting Information for Oscillatory Enzyme Dynamics Revealed by ...
Supporting Information for Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy Philip Pagano, Qi Guo, Amnon Kohen and Christopher M. Cheatum* Department of Chemistry, University of Iowa, Iowa City, IA 52242, United States *To whom correspondence should be addressed.
Figure S1. 2D IR spectra of azide bound to ternary complexes of FDH with NAD+ and NADH at T= 0, 2.5, and 5 ps plotted in -DOD from top to bottom. The purple circles are the center-line points obtained from taking slices in ω1 and finding the minimum value. The solid white line is the fit to the centerline.
Figure S2. Amplitude of the 1-2 transition as a function of T for azide bound to ternary complexes of FDH with NAD+. The peak amplitude for each spectrum is found by fitting the 1-2 transition to a 2-dimensional Gaussian function and taking the amplitude from the fit at each waiting time. Unlike the CLS, the peak amplitude does not oscillate as a function of T.
Figure S1. 2D IR spectra of azide bound to ternary complexes of FDH with NAD+ and NADH at T= 0, 2.5, and 5 ps plotted in -DOD from top to bottom. The purple circles are the center-line points obtained from taking slices in ω1 and finding the minimum value. The solid white line is the fit to the centerline.
Figure S2. Amplitude of the 1-2 transition as a function of T for azide bound to ternary complexes of FDH with NAD+. The peak amplitude for each spectrum is found by fitting the 1-2 transition to a 2-dimensional Gaussian function and taking the amplitude from the fit at each waiting time. Unlike the CLS, the peak amplitude does not oscillate as a function of T.
