UM LSA
   
   
 

faculty

  Kate Carroll  
  Kate Carroll

Assistant Professor of Chemistry, Research Assistant Professor, Life Sciences Institute
Ph.D., Stanford University

Biochemistry, Bioinorganic Chemistry, and Chemical Biology

Phone:  (734) 615-2739
E-mail: katesc@umich.edu

Research Group

 
         
 

The Carroll group in the Life Sciences Institute and the Department of Chemistry and at the University of Michigan integrates biochemistry, organic chemistry, and chemical biology approaches to address problems relevant to human health and disease.

Our research has two major focuses: Microbial sulfur metabolism and oxidation biology. In the host-pathogen arena, we are investigating sulfur metabolic pathways that allow Mycobacteria to persist in the human host. Our efforts in oxidation biology are directed at developing new chemical tools to identify and study post-translational modifications associated with cellular redox signaling and oxidative stress.

A hallmark of our program is the ability to make new molecules and use them for a targeted function. This philosophy allows students and postdocs in the group to take their own chemistry-based projects all the way to the biological finish line. We synthesize a variety of molecules ranging from activity-based chemical probes, small-molecule inhibitors, non-natural peptides, and also use directed evolution to generate novel catalysts. In turn, we apply a variety of biological, structural, and spectroscopic techniques to evaluate the properties and capabilities of newly synthesized molecules and catalysts in living cells.

 

 

AWARDS

  • 2006 Biological Sciences Scholar Program
  • 2006 Leukemia and Lymphoma Society Special Fellow Award
  • 2003 Damon Runyon Postdoctoral Fellow Award

 

REPRESENTATIVE PUBLICATIONS

  1. Rheddie, K. G., Seo, Y., Muse III, W. B., Leonard, S. & Carroll, K. S. (2008). A chemical approach for detecting sulfenic acid-modified proteins in living cells. Mol. BioSyst., DOI: 10.1039/b719986d Journal Link | Chemical Biology News | Nature Chemical Biology Highlight

  2. Chang, M. W., Belew, R. K., Carroll, K. S. , Olson, A. J. & Goodsell, D. S (2008). Empirical entropic contributions in computational docking: Evaluation in APS reductase complexes. J. Comp. Chem., DOI 10.1002/jcc.20936a Pubmed Link

  3. Bhave, D. P., Muse III, W. B. & Carroll, K. S. (2007). Drug targets in mycobacterial sulfur metabolism. Infectious Disorders - Drug Targets, 7, 140-158. Pubmed Link

  4. Chartron, J., Shiau, C., Stout, C. D., & Carroll, K. S. (2007). 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle. Biochemistry Accelerated Publication 46, 3942-3951. Pubmed Link

  5. Gao, H., Leary, J. A., Carroll, K. S., Bertozzi, C. R., & Chen, H. (2007). Noncovalent complexes of APS Reductase from Mycobacterium tuberculosis: delineating a mechanistic model using ESI-FTICR MS. J. Am. Soc. Mass Spectrom., 18, 167-178. PubMed Link | On the Cover

  6. *Charton, J., *Carroll, K. S., Shiau, C., Gao, H., Leary, J. A., Bertozzi, C. R., & Stout, C. D. (2006). Substrate recognition, protein dynamics and novel iron-sulfur cluster in Pseudomonas aeruginosa APS reductase. J. Mol. Bio., 364, 152-169. PubMed Link

  7. Carroll, K. S., Gao, H., Chen, H. Y., Leary, J. A., & Bertozzi, C. R. (2005). Investigation of the iron-sulfur cluster in Mycobacterium tuberculosis APS reductase: Implications for substrate binding and catalysis. Biochemistry, 44, 14647-14657. PubMed Link | Biochemistry Hot Article

  8. Carroll, K. S., Gao, H., Chen, H. Y., Stout, C. D., Leary, J. A., & Bertozzi, C. R. (2005). A conserved mechanism for sulfonucleotide reduction. PLOS Biology, 3, 1418-1435. PubMed Link | PLoS Synopsis | Nature Chemical Biology Highlight
         
 

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