Enzyme Models

Synthetic Models of Metalloenzymes

Living things derive energy from sunlight. Photosynthetic organisms store the energy from absorbed photons as chemical potential energy in biomolecules such as carbohydrates, fatty acids, and proteins. The chemical reactions required for biological energy storage are catalyzed by enzymes, many of which are metalloenzymes, which rely on metal ions or organometallic cofactors.

chemical structure of chlorophyll-d

Enzymes are large molecules containing hundreds or thousands of amino acid residues. Each enzyme has a small pocket—an active site—where chemical reactions occur. Because of the large size of enzyme molecules, they are challenging to study using spectroscopy, crystallography, and other chemical characterization techniques.

chemical structures of [FeFe]-hydrogenase cofactor and lactate racemase cofactor

Our approach to learning more about metalloenzymes is to synthesize small molecules designed to mimic the structure of the active sites and metallic cofactors of the enzymes. Our synthetic models are easier to characterize than whole enzymes, allowing us to more easily determine how the active sites catalyze important reactions. Our models help us understand enzymatic mechanisms, the step-by-step process by which enzymes make and break chemical bonds to store or release energy.

Interested in this project?

If you’re a SUNY Geneseo student interested in participating in this research project, please contact Dr. Tate. This project is great for biochemistry majors, especially those who are interested in chemical synthesis, biomimetic chemistry, bioinorganic chemistry, catalysis, enzymology, and sustainable energy. Preference may be given to students pursuing degrees in chemistry and biochemistry, but all students are welcome to inquire about research opportunities.