Dr. Laura Hunsicker-WangAssistant Professor, ChemistryTrinity UniversityOne Trinity PlaceSan Antonio, TX 78212-7200phone: (210) 999-7895fax: (210) 999-7569office: Moody Engineering Building 215ALaura.hunsickerwang@trinity.edu
General Research Interests:Biochemistry and Bioinorganic Chemistry Research in the Hunsicker-Wang laboratory will focus on studying enzymes that utilize or bind metal ions, called metalloproteins. There are two major areas of interest: iron-sulfur cluster enzymes and copper chaperones. Copper chaperones Metal ions inside of a cell can play one of two roles. They can be found at the active site of an enzyme, and play critical roles in the life of a cell. However, if the metal ions are left free, they can do damage to critical cellular parts. For this reason, a system of proteins called chaperones have evolved, which bind and deliver metal ions to their respective metalloprotein. One family of these chaperones is the coppers chaperones, which shuttle copper ions to Cu/Zn Super Oxide Dismutase (SOD), Fet3, and cytochrome c oxidase. The research in the Hunsicker-Wang lab will work toward identifying, purifying, and characterizing copper chaperones from the thermophilic eubacterium, Thermus thermophilus. We will also explore how copper chaperones select for only copper. Rieske proteins Iron-sulfur proteins make up ~30% of all metalloproteins. These proteins utilize iron and sulfur atoms that are organized into clusters. These proteins are often involved in electron transfer reactions. Specifically, the Rieske protein contains a 2Fe-2S cluster, which is ligated to the protein via 2 cysteine and 2 histidine residues. The reduction potential of this protein depends on the organism and the type of system that it was derived from. Previous studies have shown that the number of hydrogen bonds to the cluster, the solvent accessibility, and the type of charge residues near the cluster all affect the reduction potential. Research on this protein will involve making site-specific mutations, purifying, crystallizing and solving the structure of the mutant enzymes. The reduction potentials of these mutants will also be evaluated. Future studies will work toward evolving a new function of a larger enzyme complex, called a dioxygenase, which has a Rieske domain. The new function would be to break down environmental pollutants, and would be accomplished by making randomized mutations to both the Rieske domain and the substrate-binding domain. To see more on these research topics, go to research interests.
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