Jason M. Shearer

Assistant Professor

Inorganic, Bioinorganic, and Bioorganic Chemistry

B.S. (1998), University of Maryland, College Park; Ph.D. (2001), University of Washington (J. A. Kovacs); NIH Postdoctoral Fellow (2002-2004), Johns Hopkins University (K. D. Karlin)

E-mail: shearer [at] unr.edu
Phone: 775-784-7785
FAX: 775-784-6804
Office: CB 225

Jason M. Shearer

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Research Interests

Many of life's most important processes are performed by metalloproteins. Metalloproteins are proteins that contain one or more metal cofactors at their active-sites, and can be thought of as the ultimate transition metal complex. The ligand environment about the metal-center in a metalloprotein is often characterized by low symmetry, an unusual coordination geometry, and unique metal-ligand bonding. Therefore, many of the fine details concerning how interactions between the primary and secondary coordination sphere and the metal ion contribute to the metalloproteins physical properties and function in many metalloproteins remain unclear. To understand these complex and fascinating systems the Shearer group utilizes a multi-tiered approach. We first start by considering the relevant information concerning the metalloprotein in question and design and prepare small transition metal complexes and metallopeptides based on the active-site of the metalloprotein. These metalloprotein synthetic analogues are then subjected to a detailed spectroscopic and computational analysis. Finally the information acquired from these studies are applied back to the metalloprotein. Further studies on the metalloprotein then aid in refining future generations of the synthetic analogues, and the whole process is repeated. Current areas of focus in the Shearer group concern: the biological chemistry of nickel containing metalloproteins, the interaction between copper ions and proteins involved in neurodegenerative disorders, and the biological chemistry of sulfur and selenium containing proteins.

XAS example

Selected Publications

“The amyloid-β peptide of Alzheimer's disease binds CuI in a linear bis-His coordination environment: Insight into a possible neuroprotective mechanism for the amyloit-β peptide,” Shearer, J.; Szalai, V.A. J. Am. Chem. Soc. 2008, 130, 17826.

“Influence of Sequential Guanidinium Methylation on the Energetics of the Guanidinium...Guanine Dimer and Guanidinium...Guanine...Cytosine Trimer: Implications For the Control of Protein...DNA Interactions By Arginine Methyltransferases,” Shearer, J. J. Phys. Chem. B 2008, 112, 16997.

“Both Met(109) and Met(112) are utilized for Cu(II) coordination to the amyloidogenic fragment of the human prion protein,” Shearer, J.; Soh, P.; Lentz, S. J. Inorg. Biochem. 2008, 102, 2103.

“Probing Variable Amine/Amide Ligation in NiIIN2S2 Complexes Using Sulfur K-Edge and Nickel L-Edge X-ray Absorption Spectroscopies: Implications for the Active-Site of Nickel Superoxide Dismutase,” Shearer, J.; Dehestani, A.; Abanda, F. Inorg. Chem. 2008, 47, 2649.

“Diversity, function, and evolution of genes coding for putative Ni-containing superoxide dismutases,” Dupont, C.; Neupane, K.; Shearer, J; Palenik, B. Environ. Microbiol. 2008, 10, 1831.

“Probing Variable Axial Ligation in Nickel Superoxide Dismutase Utilizing Metallopeptide Based Models: Insight into the Superoxide Disproportionation Mechanism,” Neupane, K.P.; Gearty, K.; Francis, A.; Shearer, J. J. Am. Chem. Soc. 2007, 129, 14605.

“The Cu(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox active at physiological pH,” Shearer, J.; Soh, P. Inorg. Chem. 2007, 46, 710-719.

“Ni K-edge XAS Suggests That Coordination of Ni(II) to the Unstructured Amyloidogenic Region of the Human Prion Protein Produces a Ni2 Bis-μ-hydroxo Dimer,” Shearer, J.; Soh, P. J. Inorg. Biochem. 2007, 101, 370.

“The influence of amine/amide vs. bis-amide coordination in nickel superoxide dismutase,” Neupane, K.P.; Shearer, J. Inorg. Chem. 2006, 45, 10552-10566.

“[Me4N](NiII(BEAAM)): A synthetic model for nickel superoxide dismutase that contains Ni in a mixed amine/amide coordination environment,” Shearer, J.; Zhao, N. Inorg. Chem. 2006, 45, 9637-9639.

“Manganese Complexes of 1,3,5-Triaza-7-phosphaadamantane (PTA): The First Nitrogen-Bound Transition-Metal Complex of PTA,” Frost, B.J.; Bautista, C.M.; Huang, R.; Shearer, J. Inorg. Chem. 2006, 45, 3481.

“A nickel superoxide dismutase maquette that reproduces the spectroscopic and functional properties of the metalloenzyme,” Shearer, J.; Long, L.M. Inorg. Chem. 2006, 45, 2358-2360.

“Synthesis, characterization, and crystal structure of a quadruply bonded dimolybdenum(II) complex containing the water-soluble phosphine 1,3,5-triaza-7-phosphaadamantane (PTA),” Frost, B.J.; Miller, S.B.; Rove, K.O.; Pearson, D.M.; Korinek, J.D.; Harkreader, J.L.; Mebi, C.A.; Shearer, J. Inorg. Chim. Acta 2006, 359, 283.