Matthew D. Liptak

Professor – Inorganic Chemistry

Alma mater(s)
  • B.A., Hamilton College, Clinton, NY, 2003
  • Ph.D., University of Wisconsin, Madison, WI, 2008
  • NIH NRSA Postdoctoral Research Fellow, University of Rochester, Rochester, NY, 2008–2011

Courses

  • Chem 031 — General Chemistry 1 (Fall 2015, Spring 2017)
  • Chem 131 — Inorganic Chemistry (Spring 2018, 2020)
  • Chem 231 — Advanced Inorganic Chemistry (Fall 2011-2014, 2016-2019)
  • Chem 236 — Physical Inorganic Chemistry (Spring 2012, 2014, 2016, 2019)

Publications

Publications (from the Liptak Group webpage)

Awards and Achievements

  • New Talent: Americas, 2016
  • Paul Saltman Award, 2015
  • Ruth Kirschstein-NRSA, 2009
  • Barry M. Goldwater Scholarship, 2002

Area(s) of expertise

Bioinorganic chemistry, magneto-optical spectroscopy, computational chemistry.

Courses

  • Chem 031 — General Chemistry 1 (Fall 2015, Spring 2017)
  • Chem 131 — Inorganic Chemistry (Spring 2018, 2020)
  • Chem 231 — Advanced Inorganic Chemistry (Fall 2011-2014, 2016-2019)
  • Chem 236 — Physical Inorganic Chemistry (Spring 2012, 2014, 2016, 2019)

Awards and Achievements

  • New Talent: Americas, 2016
  • Paul Saltman Award, 2015
  • Ruth Kirschstein-NRSA, 2009
  • Barry M. Goldwater Scholarship, 2002

Areas of Expertise

Bioinorganic chemistry, magneto-optical spectroscopy, computational chemistry.

Research and/or Creative Works

Current thinking is that over a quarter of all proteins require a metal. These metalloproteins have diverse biological functions, including: oxygen transport, electron transfer, and enzyme catalysis. The Liptak group is particularly interested in elucidating the mechanisms of metalloenzymes that rely upon transition metals such as iron, cobalt, and nickel. Currently, the major thrust of the research group is unravelling the mechanisms of heme iron acquisition by pathogenic bacteria to lay the foundation for future antibiotic development. A second research focus of the group is revealing the mechanisms of metal tetrapyrrole biosynthesis with the long-term goal of designing synthetic enzymes for production of catalysts with alternative energy applications.

Chemistry diagram


Mycobacterium tuberculosis MhuD can bind one or two heme molecules

One of the major challenges for understanding metalloenzyme function is the role of electronic structure. Transition metals have the unique ability to adopt numerous oxidation, spin, and configurational states under ambient conditions and each of these electronic states has unique reactivity. In other words, simply knowing which metal is bound to an enzyme is not enough to predict its chemical reactivity! The Liptak group has developed diverse biochemical (recombinant protein expression, purification, and air-sensitive sample handling), spectroscopic (fluorescence -> electron paramagnetic resonance; time-dependent density functional theory -> hybrid quantum mechanics / molecular mechanics.), as well as computational (density functional theory, time-dependent density functional theory, and multi-reference perturbation theory) expertise to address these complex problems.
 

molecules diagram

Researchers in the Liptak group learn a variety of biochemical, spectroscopic, and computational skills in addition to management of a research project from the first experiments to journal publication. As a result, graduate student alumni have secured jobs in both academia and industry. The majority of undergraduate alumni have moved on to graduate programs in chemistry.