Linda C. Kurz, Ph.D Linda C. Kurz, Ph. The origin of the extraordinary catalytic power of enzymes continues as one of the major questions in biochemistry. We use techniques such and FTIR and NMR spectroscopy sensitive to local bond distortions, electronic environment, and other factors likely to reflect operation of the catalytic machinery.
Major projects are underway with citrate synthase and adenosine deaminase.
NMR and FTIR methods are providing information on the electronic environment and bond order substrates, groundstate and transition-state analogs when bound in the active sites of these enzymes. Using the techniques of site-directed mutagenesis to selectively alter residues in the active site, our focus now is on determining how the enzyme achieves this extraordinary substrate destabilization. The catalytic strategy of adenosine deaminase involves the stabilization of a tetrahedral intermediate. Recently, we have trapped and observed the formation of an analog of this intermediate. A Analog-Citrate Synthase Complexes.