The University of Iowa

Christopher M. Cheatum

Christopher M. Cheatum
Associate Professor
326 IATL
Office Hours: 
Tuesday and Wednesday 1:30-3:00
  • 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.

Research Interests: 

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. 

Recent Publications: 
  • 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.M2D 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.