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Jason Shearer

Associate Professor

Contact Information


  • 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


  • J. Shearer, “Insight Into The Structure and Mechanism of Nickel Containing Superoxide Dismutase Derived From Peptide Based Mimics.” Acc. Chem. Res., 2014, 47, 2332-2341. (DOI: 10.1021/ar500060s)
  • J. Shearer, “Use of Metallopeptide Based Mimics Suggests A Proton Coupled Electron Transfer Mechanism During Superoxide Reduction Facilitated by Nickel Containing Superoxide Dismutase.” Angew. Chem., Int. Ed., 2013, 52, 2569–2572. (DOI: 10.1002/anie.201209746)
  • J. Shearer, P. E. Callan, C. A. Masitas and C. Grapperhaus, “Influence of Sequential Thiolate Oxidation on a Nitrile Hydratase Mimic Probed by Multiedge X-ray Absorption Spectroscopy.” Inorg. Chem., 2012, 51, 6032-6045. (DOI: 10.1021/ic202453c)
  • J. Shearer, P. E. Callan and J. Amie, “Metallopeptide Based Mimics Demonstrates That the Metalloprotein Nitrile Hydratase Requires Two Oxidized Cysteinates for Catalytic Activity.” Inorg. Chem., 2010, 49, 9064-9077. (DOI: 10.1021/ic101765h)
  • J. Shearer, K. P. Neupane and P. E. Callan “Use of N-Substitute Histidines in Metallopeptide Based Models To Mimic the Hydrogen-Bonding Network to the Coordinated Imidazole in Nickel-Containing Superoxide Dismutase: Role of a Key Hydrogen Bonding Network in the Metalloenzyme.” Inorg. Chem., 2009, 48, 10560-10571. (DOI: 10.1021/ic9010407)
  • J. Shearer and V. A. Szalai, “The Amyloid-β peptide of Alzheimer’s Disease Binds CuI in a Linear Bis-His Coordination Environment: Insight Into a Possible Neuroprotective Mechanism.” J. Am. Chem. Soc., 2008, 130, 17826- 17835. (DOI: 10.1021/ja805940m)
  • K. P. Neupane, K. Gearty, A. Francis and J. Shearer “Variable Axial Ligation in Nickel Superoxide Dismutase Utilizing Metallopeptide Based Models: Insight into the Superoxide Disproportionation Mechanism.” J. Am. Chem. Soc., 2007, 129, 14605-14618. (DOI: 10.1021/ja0731625)
  • J. Shearer and L. M. Long, “A Nickel Superoxide Dismutase Maquette That Reproduces the Spectroscopic and Functional Properties of the Metalloenzyme.” Inorg. Chem., 2006, 45, 2358-2360. (DOI: 10.1021/ic0514344)
  • J. Shearer, A. Dehestani and F. Abanda, “Probing Variable Amine/Amide Coordination in NiIIN2S2 Complexes using Nickel L-edge and Sulfur K-edge X-ray Absorption Spectroscopy: Implications for the Active-Site of Nickel Superoxide Dismutase.” Inorg. Chem., 2008, 47, 2649-2660. (DOI: 10.1021/ic7019878)

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