Office: 409 Science & Technology Building
Email: firstname.lastname@example.org Lab Website: http://blog.ecu.edu/sites/offenbacherlabecu
NIH F32 Postdoctoral Fellow, University of California, Berkeley (2015-2017)
Postdoctoral Fellow, University of California, Berkeley (2013-2015)
Postdoctoral Fellow, Georgia Institute of Technology (2011-2013)
Ph.D., Chemistry, Georgia Institute of Technology (2005-2011)
B.S.,Biochemistry, Ohio Northern University (2001-2005)
Assistant Professor of Biochemistry
Research in the Offenbacher lab is centered on elucidating the molecular underpinnings of biological catalysis. There are two main areas of research in our lab. First is to uncover how conformational flexibility is related to enzyme catalysis. These details will enrich our understanding of the origins of the enormous catalytic proficiencies of natural enzymes and yield blueprints for future biological catalyst design. The dynamic properties of proteins are also studied in the context of allostery and the molecular basis of mutation linked diseases. Second is to develop novel kinetic and/or spectroscopic probes for mechanistic interrogation of proton-coupled electron transfer in enzyme function.
The projects combine interdisciplinary study across fields including enzymology, chemical, molecular and structural biology, and biophysical chemistry. A focus is centered on training and engaging students in practical laboratory investigations, relevant to modern biochemistry, using various biochemical and structural/biophysical techniques(e.g. protein expression and purification; enzyme kinetics; site-directed mutagenesis; hydrogen deuterium exchange mass spectrometry, HDXMS; vibrational,fluorescence, and electron paramagnetic resonance spectroscopy).
The Offenbacher lab
currently has openings for graduate students (MS and PhD); motivated candidates
with a thirst for learning a broad range of biochemical tools to study enzyme
mechanisms should contact Dr. Offenbacher. Click on our website link to learn
Adam R. Offenbacher, Shenshen Hu, Erin M.Poss, Cody A. M. Carr, Alexander D. Scouras, Anthony T. Iavarone, Ali Palla,Tom Alber, James S. Fraser, and Judith P. Klinman. Hydrogen deuterium exchange uncovers a relationship between distal, solvent exposed protein motions and the thermal activation barrier for catalytic proton-coupled electron tunneling. ACS Cent.Sci. 2017, 3, 570-579.
(Masaki Horitani, Adam R. Offenbacher), Cody A. M. Carr, Tao Yu,Sharon Hammes-Schiffer, Judith P. Klinman, and Brian M. Hoffman. Active site structure of a lipoxygenase-substrate complex from 13C ENDOR spectroscopy reveals structural basis for tunneling properties that underlie C-H activation. J. Am.Chem. Soc. 2017, 139, 1984-1997.
Adam R. Offenbacher, Brandon C. Polander, and Bridgette A. Barry. An intrinsically disordered photosystem II subunit, PsbO, provides a structural template and a sensor of the hydrogen-bonding network in photosynthetic water oxidation. J. Biol. Chem. 2013, 288, 29056-29068.
Bridgette A.Barry, Jun Chen, James Keough, David Jenson, Adam Offenbacher, and Cynthia Pagba. Proton-coupled electron transfer and redox-active tyrosines: Structure and function of the tyrosyl radicals in ribonucleotide reductase and photosystem II. J. Phys.Chem. Lett. 2012,3, 543-554.
*For a complete list, click on the link: https://www.ncbi.nlm.nih.gov/myncbi/browse/collection/53307888