个人简介

Deborah Perlstein joined the Department of Chemistry in July 2010. While new to Boston University, she has called Boston her home since arriving in the fall of 1998 to pursue her Ph.D. at MIT. More recently, she was an NIH Postdoctoral Fellow in the laboratory of Suzanne Walker in the Department of Microbiology and Molecular Genetics at Harvard Medical School.

研究领域

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Biological Chemistry

The research the Perlstein Group lies at the interface of chemistry and biology with a focus on bioinorganic chemistry. We are currently developing new projects that will use the tools of chemical biology, including biophysical techniques, enzymology, microscopy, and molecular biology to understand iron-sulfur cluster containing proteins and bacterial cell division. Using site specific substrate analogs, Prof. Perlstein was able to demonstrate distinct lipid lengths for donor and acceptor sites in peptidoglycan glycosyltransferases. Iron-sulfur proteins. Iron-sulfur clusters are ancient and essential cofactors that allow proteins to access a wide range of chemistries that would not otherwise be possible with the standard 20 amino acids. Elucidating the novel chemical mechanisms of enzymes that utilize iron-sulfur clusters and understanding the biochemical pathway required for iron sulfur cluster assembly in vivo will be a major focus of the lab’s research efforts. Bacterial Cell Division. The bacterial cytoskeletal proteins MreB and FtsZ are the major orchestrators of cell growth and division and therefore represent potential antibiotic targets that can be exploited to combat drug resistant pathogens. These bacterial homologs of actin and tubulin coordinate the activities of numerous enzymes in the cell membrane and the perplasmic space that maintain the integrity of the bacterial cell envelope during growth and division. We are developing projects to probe how cytoskeletal protein dynamics are regulated both in vitro and in vivo to discover new approaches to combating drug resistant microorganisms.