Researchers in the Suess Lab tackle problems at the interface of inorganic and biological chemistry. Many of the reactions that underlie fundamental life processes are catalyzed by metals found in the active sites of metalloenzymes. Some metalloenzyme active sites feature only a single metal ion, but hundreds of thousands feature polynuclear metallocofactors—clusters of multiple metal ions that work cooperatively to maximize catalytic efficiency and/or to achieve reactivity not possible at a single metal. Of such polynuclear metallocofactors, iron-sulfur clusters are the most ubiquitous; they are found in all kingdoms of life and are as old as life itself. They play a central role in health and metabolism and are constantly reshaping the molecular composition of the biosphere. And their reaction chemistry is as diverse as their functions: iron-sulfur clusters catalyze some of the most demanding reactions, such as the conversion of inert dinitrogen to ammonia fertilizer, as well as simpler electron-transfer reactions that support photosynthesis, respiration, and DNA repair. Given their prominent role in all facets of life, my research group studies the reaction mechanisms of iron-sulfur clusters, with a particular focus on revealing the fundamental chemical bonding that gives rise to their unusual reactivity.
The unifying goal of our research is to understand the nature of the iron-iron and iron-sulfur interactions in iron-sulfur clusters, the physical properties that emerge therefrom, and how these physical properties contribute to the reaction chemistry of iron-sulfur clusters. We study both synthetic iron-sulfur clusters—those produced in the laboratory—as well as biogenic clusters, produced in the cell. By working at this synthetic/biological interface, we forge deep connections between the properties and reactivity/functions of iron-sulfur clusters.