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 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.

“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.

“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.

“Distinguishing between rate limiting electron- versus H-atom transfer pathways in Cu2-O2 mediated oxidative N-dealkylations: Application of inter- vs. intramolecular KIEs,” Shearer, J.; Zhang, C.X.; Hatcher, L.Q.; Karlin, K.D. J. Am. Chem. Soc. 2003, 125, 12670-12671.

“Synthetic models for the non-heme metalloenzyme superoxide reductase: Observation and structural characterization by XAS of an Fe(III)-peroxo intermediate,” Shearer, J.; Scarrow, R.C.; Kovacs, J.A. J. Am. Chem. Soc. 2002, 124, 11709-11717.

“The first example of a nitrile hydratase model complex that reversibly binds nitriles,” Shearer, J.; Jackson, H.L.; Schweitzer, D.; Rittenberg, D.K.; Leary, T.M.; Kaminsky, W.; Scarrow, R.C.; Kovacs, J.A. J. Am. Chem. Soc. 2002, 124, 11417-11428.

“Why is there an ‘inert’ metal in the active-site of nitrile hydratase? Reactivity and ligand dissociation from a five-coordinate Co(III) nitrile hydratase model,” Shearer, J.; Kung, I.Y.; Lovell, S.; Kaminsky, W.; Kovacs, J.A. J. Am. Chem. Soc. 2001, 123, 463-468.

“Alkylation of nucleic acids by a model quinone methide,” Pande, P; Shearer, J.; Yang, J.; Greenberg, W.A.; Rokita, S.E. J. Am. Chem. Soc. 1999, 121, 6773-6779.