Christopher M. Cheatum
- B.S., University of New Mexico (1995)
- Ph.D., University of Wisconsin - Madison (2001)
- Postdoctoral Fellow, M.I.T. (2001-2003)
Femtosecond infrared spectroscopy of enzymes, proton-transfer reactions, molecular mechanisms of enzymatic catalysis, reaction dynamics in proteins, vibrational spectroscopy and dynamics, nonlinear spectroscopy.
The protein environment of enzyme active sites is important in facilitating enzymatic reactions. The protein binds the substrate holding it in a particular geometry so that nearby functional groups are oriented to stabilize the transition state. These functional groups are involved in the reaction mechanism acting as hydrogen-bond partners, providing an electrostatic environment favorable for the reaction, and taking part as acidic or basic groups in proton-transfer reactions. The reaction kinetics are controlled by these local interactions with the protein. This static picture of the protein/substrate interactions, however, is an incomplete description of the catalytic process because fluctuations of these protein functional groups can also be important in the reaction mechanism. In enzymatic hydrogen-transfer reactions, for example, fluctuations of the protein can cause a time-dependent variation in the donor-acceptor separation resulting in large changes in the hydrogen-transfer barrier height. We use 2D IR correlation spectroscopy to study the fluctuations of the enzyme active site and the specific interactions that control the chemistry.
- Dutta, S.; Yun-Liang, L.; Houtman, J.C.D.; Kohen, A.; Cheatum, C.M. 3-Picolyl Azide Adenine Dinucleotide as a Probe of Femtosecond to Picosecond Time Scale Enzyme Dynamics. J. Phys. Chem B 2012, 116, 542-548.
- Dutta, S.; Rock, W.; Cook, R.J.; Kohen, A.; Cheatum, C.M. 2D IR Spectroscopy of Azido-Nicotinamide Adenine Dinucleotide in Water. J. Chem. Phys 2011, 135, 055106-6.
- Nydegger, M.; Rock, W.; Cheatum, C.M. 2D IR Spectroscopy of the C-D Stretching Vibration of the Deuterated Formic Acid Dimer. Chem. Phys. 2011,13, 6098-6104.
- Bandaria, J.N.; Dutta, S.; Nydegger, M.; Rock, W.; Kohen, A.; Cheatum, C.M. Characterizing the Dynamics of Functionally Relevant Complexes of Formate Dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 17974-17979.
- Dutta, S.; Cook, R.J., Houtman J.C.D.; Kohen, A.; Cheatum, C.M. Characterization of Azido-NAD+ to Assess its Potential as a 2D IR Probe of Enzyme Dynamics. Analytical Biochem. 2010, 407, 241-246.
- Nydegger, M.; Dutta, S.; Cheatum, C.M. 2D IR Study of 3-Azidopyridine as a Potential Spectroscopic Reporter of Protonation State. J. Chem. Phys. 2010,133, 134506-1–134506-8.
- Zimmermann, J.; Gundogdu, K.; Cremeens, M.E., Bandaria, J.N.; Hwang, G.T.; Thielges, M.C.; Cheatum, C.M.; Romesberg, F.E. Efforts Toward Developing Probes of Protein Dynamics: Vibrational Dephasing and Relaxation of Carbon-Deuterium Stretching Modes in Deuterated Leucine. J. Phys. Chem. B 2009, 113, 7991-7994.
- Hill, S.E.; Bandaria, J.N.; Fox, M.; Vanderah, E.; Kohen, A.; Cheatum, C.M. Exploring the Molecular Origins of Protein Dynamics in the Active Site of Human Carbonic Anhydrase II. J. Phys. Chem B 2009, 113, 11505-11510.
- Hill, S.E.; Kohen, A.; Cheatum, C.M. Fast Enzyme Dynamics at the Active Site of Formate Dehydrogenase. J. Am. Chem. Soc. 2008, 130, 22-23.
- Gundogdu, K.; Bandaria, J.N.; Nydegger, M.; Rock, W.; Cheatum, C.M. Relaxation and Anharmonic Couplings of the O-H Stretching Vibration of Asymmetric Strongly Hydrogen-Bonded Complexes. J. Chem. Phys. 2007, 127, 044501.