Aaron Lucius. Professor; Graduate Program Director
Chemistry Building 292
(205) 934-8096

Research and Teaching Interests: Physical Chemistry, Biophysical Chemistry, Thermodynamics of Protein-protein and Protein-ligand Interactions, Pre-steady State Kinetics, Enzyme Mechanism, and Motor Proteins

Office Hours: By appointment

  • BS, Oregon State University, Biochemistry and Biophysics
  • PhD, Washington University School of Medicine in St. Louis, Molecular Biophysics

I am from the Pacific Northwest and received my bachelors in Biochemistry and Biophysics from Oregon State University in Corvallis, Oregon. During my time there, I did undergraduate research to examine the pre-steady state kinetic mechanism of DNA insertion catalyzed by retroviral integrase. I became intensely interested in enzyme mechanism and joined Tim Lohman’s group in the Department of Biochemistry and Molecular Biophysics at Washington University School of Medicine in St. Louis. I received my PhD in Molecular Biophysics in 2003. This was followed by postdoctoral research under the direction of Wlodek Bujalowski at the University of Texas Medical Branch (UTMB) in Galveston, Texas.

My training experiences provided skills in the application of thermodynamic and rapid-mixing kinetic techniques to examine enzyme mechanism. In 2006 I joined the UAB Department of Chemistry as an Assistant professor. My research has been focused on understanding the molecular mechanisms of motor proteins. The work has been funded by both the NSF and NIH. I was promoted to full professor in 2015 and have graduated five PhD students in my nine year tenure during which time I was presented with the Dean’s Award for Excellence in Mentorship award.

The fundamental question that my group seeks to address is, how does a motor protein couple the energy from ATP binding and hydrolysis to perform mechanical work? To address this question we use chemical quenched-flow and fluorescence stopped-flow assays. Both techniques allow us to rapidly mix two reagents within 2 ms and observe a reaction on the millisecond time scale, which, in most cases, is the appropriate temporal resolution for enzyme catalysis.

To both design and interpret the rapid mixing kinetic experiments, one requires knowledge of the energetics of the binding and assembly reactions that occur. To address these questions, we use an array of thermodynamic, hydrodynamic, and spectroscopic approaches. These include analytical ultracentrifugation, dynamic and static light scattering, fluorescence titrations, and isothermal titration calorimetry (ITC), among others.

Just like physics seeks to describe phenomena with mathematics, biophysics seeks to describe molecular level events with mathematics. Thus, a major component of our work is using mathematics to quantitatively describe the observed physical phenomena. This is accomplished by using tools like Mathematica and Matlab to solve complex systems of both coupled differential and coupled algebraic equations. The derived solutions can then be used to model and describe the experimental results. This can often require coding in Matlab, C++, or Fortran.

In total, the research truly lies at the interface between Chemistry, Biology, Physics, and Mathematics. There is a place in my research group for members from each discipline.
  • CH 325: Physical Chemistry 1 (Thermodynamics and Kinetics)
  • CH 700: Foundations of Physical and Analytical Chemistry
  • CH 493: Biochemistry Laboratory
  • Lin, J.; Lucius, A. L. Examination of the Dynamic Assembly Equilibrium for E. coli ClpB. Proteins 2015, in press. DOI: 10.1002/prot.24914
  • Li, T.; Weaver, C. L.; Lin, J.; Duran, E.; Miller, J. M.; Lucius, A. L. E. coli ClpB is a Non-Processive Polypeptide Translocase. Biochemical Journal 2015, 470(1), 39-52.
  • Li, T.; Lin, J.; Lucius, A. L. Examination of polypeptide substrate specificity for Escherichia coli ClpB. Proteins 2015, 83(1), 117-134.
  • Miller, J. M.; Lucius, A. L. ATPγS Competes with ATP for Binding at Domain 1 but not Domain 2 during ClpA Catalyzed Polypeptide Translocation. Biophysical Chemistry 2014, 185, 58-69.
  • Miller, J. M.; Lin, J.; Li, T.; Lucius, A. L. E. coli ClpA Catalyzed Polypeptide Translocation is Allosterically Controlled by the Protease ClpP. Journal of Molecular Biology 2013, 425, 2795-2812.
  • Li, T.; Lucius, A. L. Examination of Polypeptide Substrate Specificity for E. coli ClpA. Biochemistry 2013, 52, 4941-4954.
  • Veronese, P. K.; Rajendar, B.; Lucius, A. L. Activity of E. coli ClpA Bound by Nucleoside Di- and Triphosphates. J. Mol. Biol. 2011, 409, 333-47.
  • Veronese, P. K.; Lucius, A. L. Effect of Temperature on the Assembly of the Escherichia coli ClpA Molecular Chaperone. Biochemistry 2010, 49, 9820-9829.
  • Rajendar, B.; Lucius,  A. L. Molecular Mechanism of Polypeptide Translocation Catalyzed by the E. coli ClpA Protein Translocase. J. Mol. Biol. 2010, 399, 665-679.  This article was featured on the cover of J. Mol. Biol. and a commentary was written on the manuscript see T.M. Lohman “Clipping Along” J. Mol. Biol 2010, 399, 663-4.
Full Publication List
  • American Chemical Society (ACS)
  • Biophysical Society
  • Society for Advancement of Hispanics/Chicanos and Native Americans in Science (SACNAS)

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