William L. Mock

Professor

Organic Chemistry

My interests cover a range of research areas, encompassing projects in synthesis of novel carbocyclic and heterocyclic structures as well as studies in the mechanism of organic reactions. Recently I have focused on the subject of enzyme mechanisms, trying to understand the origins of selectivity and efficiency. My research group is examining the kinetics of metalloproteases such as carboxypeptidase A, a proteolytic enzyme common to mammalian digestive systems. We are carrying out selective chemical modifications of the active site region of the enzyme. Resulting catalytic properties of the enzyme allow mechanistic deductions to be drawn. We also design, synthesize, and test substrate analogs, with the same goal. Much of our work involves development of novel principles of enzyme inhibition, with potential biomedical applications.

We are also involved in molecular recognition chemistry, the study of noncovalent binding of small organic molecules to larger organic species having cavities within them. We are able to prepare a nonadecacyclic cage structure (cucurbituril), which is a successful enzyme mimic. It catalyzes a cycloaddition between an azide and an alkyne, yielding a triazole. Saturation kinetics are observed, and detailed investigation allows comprehension of the factors contributing to reaction rate acceleration.