Rate My Professor Matthew Liptak

Matthew D. Liptak is a Professor of Inorganic Chemistry in the Department of Chemistry at the University of Vermont, where he joined the faculty as an Assistant Professor in 2011, was promoted to Associate Professor in 2018, and became full Professor in 2022. He currently serves as Director of the Biochemistry B.S. Program since 2021 and previously coordinated the Chemistry Ph.D. and M.S. programs from 2017 to 2021. Liptak earned a B.A. in Chemistry with a minor in Physics from Hamilton College in 2003 and a Ph.D. in Physical Chemistry from the University of Wisconsin-Madison in 2008, advised by Professor Thomas C. Brunold. He then held an NIH Ruth Kirschstein NRSA Postdoctoral Research Fellowship at the University of Rochester from 2008 to 2011, working with Professor Kara L. Bren on NMR and DFT investigations of porphyrin conformation in cytochromes c.

Liptak's research centers on bioinorganic chemistry, magneto-optical spectroscopy, and computational chemistry, with a focus on elucidating the mechanisms of metalloenzymes that rely on transition metals such as iron, cobalt, and nickel. His group investigates heme degradation pathways in pathogenic bacteria, including enzymes IsdG from Staphylococcus aureus and MhuD from Mycobacterium tuberculosis, to inform novel antibiotic development; class II chelatases involved in metal tetrapyrrole biosynthesis for designing synthetic enzymes in alternative energy applications; and molecular photophysics, including mechanisms of aggregation-induced emission and large Stokes shifts in fluorophores. He has secured major funding, including the NIGMS MIRA Award totaling $1,389,462 from 2021 to 2026 and an NSF grant of $399,000 from 2020 to 2023. Liptak has received the UVM College of Arts and Sciences Dean’s Teacher-Scholar Award, election to the Vermont Academy of Science and Engineering, New Talent: Americas Award in 2016, and Paul Saltman Award in 2015. Key publications include “Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin” (Journal of Biological Inorganic Chemistry, 2022), “A dynamic substrate is required for MhuD-catalyzed degradation of heme to mycobilin” (Biochemistry, 2021), “Suppression of Kasha’s Rule (SOKR): A Novel Mechanism to Explain Aggregation Induced Emission” (Nature Chemistry, 2017), and “Dynamic Ruffling Distortion of the Heme Substrate in Non-Canonical Heme Oxygenase Enzymes” (Dalton Transactions, 2016).