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Jason M. Shearer

Associate Professor

Contact Information

Degrees

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

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.
Jason Shearer

Publications

  • Shearer, J., Callan, P. E., Masitas, C. A., Grapperhaus, C. A. Influence of Sequential Thiolate Oxidation on a Nitrile Hydratase Mimic Probed by Multi-edge X-ray Absorption Spectroscopy. Inorganic Chemistry, 2012, 51, 6032-6045.
  • Tran, N. G., Kalyvas H., Skodje, K. M., Hayashi, T., Moënne-Loccoz, Callan, P. E., Shearer, J., Kirschenbaum, L. J., Kim, E. Phenol Nitration Induced by an {Fe(NO)2}10 Dinitrosyl Iron Complex. J. Am. Chem. Soc., 2011, 133, 1184-1187.
  • Tran, T.; Szalai, V. A.; Shearer, J. M.; Callan, P. E. Cu K-edge X-ray Absorption Spectroscopy Reveals Differential Copper Coordination Within Amyloid-β Oligomers Compared to Amyloid-β Monomers. Chem. Comm. 2010, 46, 9137-9139.
  • Shearer, J. M.; Callan, P. E.; Amie, J. Metallopeptide Based Mimics Demonstrates That the Metalloprotein Nitrile Hydratase Requires Two Oxidized Cysteinates for Catalytic Activity. Inorg. Chem. 2010, 49, 9064-9077.
  • Lesh, F. D.; Shanmugam, R.; Allard, M. M.; Lanznaster, M.; Hegg, M. J.; Rodgers, M. T.; Shearer, J. M.; Verani, C. N. A Modular Approach to Redox-active Multimetallic Amphiphiles of Discotic Topology. Inorg. Chem. 2010, 49, 7226-7228.
  • Shearer, J. M.; Mathrubootham, V.; Thomas, J.; Staples, R.; McCraken, J.; Hegg, E. L. Bis-amide and Monoamine/amide NiN2S2 Complexes as Models for Nickel Containing Acetyl Coenzyme Synthase and Superoxide Dismutase: An Experimental and Computational Study. Inorg. Chem. 2010, 49, 5393-5406
  • Catalano, V. J.; Moore, A. L.; Shearer, J. M.; Kim, J. Luminescent Copper(I) Halide Butterfly Dimers Coordinated to [Au(CH3imCH2py)2]BF4 and [Au(CH3imCH2quin)2]BF4. Inorg. Chem. 2009, 48, 11362-11375.
  • Shearer, J. M.; Neupane, K. P.; Callan, P. E. Metallopeptide Based Mimics with Substituted Histidines Approximate a Key Hydrogen Bonding Network in the Metalloenzyme Nickel Superoxide Dismutase. Inorg. Chem. 2009, 48, 10560-10571.
  • Shearer, J.; Szalai, V.A. 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. J. Am. Chem. Soc. 2008, 130, 17826.
  • Shearer, J. 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. J. Phys. Chem. B 2008, 112, 16997.
  • Shearer, J.; Soh, P.; Lentz, S. Both Met(109) and Met(112) are utilized for Cu(II) coordination to the amyloidogenic fragment of the human prion protein. J. Inorg. Biochem. 2008, 102, 2103-2113.
  • Shearer, J.; Dehestani, A.; Abanda, F. 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. Inorg. Chem. 2008, 47, 2649-2660.
  • Dupont, C.; Neupane, K.; Shearer, J; Palenik, B. Diversity, function, and evolution of genes coding for putative Ni-containing superoxide dismutases. Environ. Microbiol. 2008, 10, 1831-1843.

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