Jason Shearer

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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


  • Ermert, D.M.; Ghiviriga, I.; Catalano, V.J.; Shearer, J.; Murray, L.J.  An Air- and Water-​Tolerant Zinc Hydride Cluster That Reacts Selectively With CO2Angew. Chem., Int. Ed. 2015, 54, 7047-7050.
  • Shearer, J.; Schmitt, J.C.; Clewett, H.S.  Adiabaticity of the Proton-​Coupled Electron-​Transfer Step in the Reduction of Superoxide Effected by Nickel-​Containing Superoxide Dismutase Metallopeptide-​Based Mimics.  J. Phys. Chem. B 2015, 119, 5453-5461.
  • Gan, L.; Groy, T.L.; Tarakeshwar, P.; Mazinani, S.K.S.; Shearer, J.; Mujica, V.; Jones, A.K.  A Nickel Phosphine Complex as a Fast and Efficient Hydrogen Production Catalyst.  J. Am. Chem. Soc. 2015, 137, 1109-1115.
  • Shearer, J.; Peck, K.L.; Schmitt, J.C.; Neupane, K.P.  Cysteinate protonation and water hydrogen bonding at the active-​site of a nickel superoxide dismutase metallopeptide-​based mimic:  Implications for the mechanism of superoxide reduction.  J. Am. Chem. Soc. 2014, 136, 16009-16022.
  • Murray, L.J.; Weare, W.W.; Shearer, J.; Mitchell, A.D.; Abboud, K.A.  Isolation of a (Dinitrogen)​Tricopper(I) Complex.  J. Am. Chem. Soc. 2014, 136, 13502-13505.
  • Lim, S.H.; Schmitt, J.C.; Shearer, J.; England, K.R.; Olmstead, M.M.; Balch, A.L.  Formation and structure of two luminescent salts of [Au(SCSN3)​2]​- obtained through the [2 + 3] cyclization of carbon disulfide and azide ion.  Dalton Trans. 2014, 43, 13756-13763.
  • Shearer, J.  Insight into the structure and mechanism of nickel-​containing superoxide dismutase derived from peptide-​based mimics.  Acc. Chem. Res. 2014, 47, 2332-2341.
  • Fitzpatrick, J.; Kalyvas, H.; Filipovic, M.R.; Ivanovic-Burmazovic, I.; MacDonald, J.C.; Shearer, J.; Kim, E.  Transformation of a Mononitrosyl Iron Complex to a [2Fe-​2S] Cluster by a Cysteine Analogue.  J. Am. Chem. Soc. 2014, 136, 7229-7232.
  • Linn, D.; Kieser, J.; Shearer, J.  The novel hydrogen-​rich binuclear cobalt complex anion, [(CoH3)​2H3]​5-Dalton Trans. 2014, 43, 3412-3415.
  • Shearer, J.  Dioxygen and superoxide stability of metallopeptide based mimics of nickel containing superoxide dismutase:  The influence of amine​/amidate vs. bis-​amidate ligation.  J. Inorg. Biochem. 2013, 129, 145-149.
  • Bellow, J.A.; Fang, D.; Kovacevic, N.; Martin, P.D.; Shearer, J.; Cisneros, G.A.; Groysman, S.  Novel Alkoxide Cluster Topologies Featuring Rare Seesaw Geometry at Transition Metal Centers.  Chem. - Eur. J. 2013, 19, 12225-12228.
  • Fitzpatrick, J.; Kalyvas, H.; Shearer, J.; Kim, E.  Dioxygen mediated conversion of {Fe(NO)​2}​9 dinitrosyl iron complexes to Roussin's red esters.  Chem. Commun. (Cambridge, U.K.) 2013, 49, 5550-5552.
  • Peck, K.L.; Clewett, H.S.; Schmitt, J.C.; Shearer, J.  Copper ligation to soluble oligomers of the English mutant of the amyloid-​β peptide yields a linear Cu(i) site that is resistant to O2 oxidation.  Chem. Commun. (Cambridge, U.K.)  2013, 49, 4797-4799.
  • Dutta, A.; Flores, M.; Roy, S.; Schmitt, J.C.; Hamilton, G.A.; Hartnett, H.E.; Shearer, J.M.; Jones, A.K.  Sequential oxidations of thiolates and the cobalt metallocenter in a synthetic metallopeptide:  Implications for the biosynthesis of nitrile hydratase.  Inorg. Chem. 2013, 52, 5236-5245.
  • Shearer, J.  Use of a Metallopeptide-​Based Mimic Provides Evidence for a Proton-​Coupled Electron-​Transfer Mechanism for Superoxide Reduction By Nickel-​Containing Superoxide Dismutase.  Angew. Chem., Int. Ed. 2013, 52, 2569-2572.
  • Lim, S.H.; Schmitt, J.C.; Shearer, J.; Jia, J.; Olmstead, M.M.; Fettinger, J.C.; Balch, A.L.  Crystallographic and Computational Studies of Luminescent, Binuclear Gold(I) Complexes, AuI2(Ph2P(CH2)​nPPh2)​2I2 (n = 3-​6).  Inorg. Chem. 2013, 52, 823-831.
  • Coggins, M.K.; Toledo, S.; Shaffer, E.; Kaminsky, W.; Shearer, J.; Kovacs, J.A.  Characterization and Dioxygen Reactivity of a New Series of Coordinatively Unsaturated Thiolate-​Ligated Manganese(II) Complexes.  Inorg. Chem. 2012, 51, 6633-6644.
  • Shearer, J.; Callan, P.E.; Masitas, C.A.; Grapperhaus, C.A.  Influence of Sequential Thiolate Oxidation on a Nitrile Hydratase Mimic Probed by Multiedge X-​ray Absorption Spectroscopy.  Inorg. Chem. 2012, 51, 6032-6045.
  • Chen, K.; Strasser, C.E.; Schmitt, J.C.; Shearer, J.; Catalano, V.J.  Modulation of Luminescence by Subtle Anion-​Cation and Anion-​π Interactions in a Trigonal AuI···CuI Complex.  Inorg. Chem. 2012, 51, 1207-1209.
  • Shakya, R.; Allard, M.M.; Johann, M.; Heeg, M.J.; Rentschler, E.; Shearer, J.M.; McGarvey, B.; Verani, C.N.  Modeling the Geometric, Electronic, and Redox Properties of Iron(III)​-​Containing Amphiphiles with Asymmetric [NN'O] Headgroups.  Inorg. Chem. 2011, 50, 8356-8366.
  • Shearer, J.; Rosenkoetter, K.E.; Callan, P.E.; Pham, C.  One Octarepeate Expansion to the Human Prion Protein Alters Both the Zn2+ and Cu2+ Coordination Environments within the Octarepeate Domain.  Inorg. Chem. 2011, 50, 1173-1175.
  • Tran, N.G.; Kalyvas, H.; Skodje, K.M.; Hayashi, T.; Moenne-Loccoz, P.; 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.
  • Shearer, J.; Callan, P.E.; Tran, T.; Szalai, V.A.  Cu K-​edge X-​ray absorption spectroscopy reveals differential copper coordination within amyloid-​β oligomers compared to amyloid-​β monomers.  Chem. Commun. (Cambridge, U.K.) 2010, 46, 9137-9139.
  • Shearer, J.; Callan, P.E.; Amie, J.  Use of 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.; Heeg, M.J.; Rodgers, M.T.; Shearer, J.M.; Verani, C.N.  A Modular Approach to Redox-​Active Multimetallic Hydrophobes of Discoid Topology.  Inorg. Chem. 2010, 49, 7226-7228.
  • Mathrubootham, V.; Thomas, J.; Staples, R.; McCraken, J.; Shearer, J.; Hegg, E.L.  Bisamidate and Mixed Amine​/Amidate NiN2S2 Complexes as Models for Nickel-​Containing Acetyl Coenzyme A Synthase and Superoxide Dismutase:  An Experimental and Computational Study.  Inorg. Chem. 2010, 49, 5393-5406.
  • Catalano, V.J.; Moore, A.L.; Shearer, J.; 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.; 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 Amyloid-​β Peptide.  J. Am. Chem. Soc. 2008, 130, 17826-17835.
  • 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, 16995-17002.
  • Shearer, J.; Soh, P.; Lentz, S.  Both Met(109) and Met(112) are utilized for Cu(II) coordination by the amyloidogenic fragment of the human prion protein at physiological pH.  J. Inorg. Biochem. 2008, 102, 2103-2113.
  • Lugo-Mas, P.; Taylor, W.; Schweitzer, D.; Theisen, R.M.; Xu, L.; Shearer, J.; Swartz, R.D.; Gleaves, M.C.; DiPasquale, A.; Kaminsky, W.; Kovacs, J.A.  Properties of Square-​Pyramidal Alkyl-​Thiolate FeIII Complexes, Including an Analogue of the Unmodified Form of Nitrile Hydratase.  Inorg. Chem. 2008, 47, 11228-11236.
  • Dupont, C.L.; 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.
  • 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.
  • Neupane, K.P.; Gearty, K.; Francis, A.; Shearer, J.  Probing 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.
  • Brines, L.M.; Shearer, J.; Fender, J.K.; Schweitzer, D.; Shoner, S.C.; Barnhart, D.; Kaminsky, W.; Lovell, S.; Kovacs, J.A. Periodic trends within a series of five-​coordinate thiolate-​ligated [MII(SMe2N4(tren)​)​]​+ (M = Mn, Fe, Co, Ni, Cu, Zn) complexes, including a rare example of a stable CuII-​thiolate.  Inorg. Chem. 2007, 46, 9267-9277.
  • Shearer, J.; Soh, P.  Ni K-​edge XAS suggests that coordination of NiII to the unstructured amyloidogenic region of the human prion protein produces a Ni2 bis-​μ-​hydroxo dimer.  J. Inorg. Biochem. 2007, 101, 370-373.
  • Shearer, J.; Soh, P.  The Copper(II) Adduct of the Unstructured Region of the Amyloidogenic Fragment Derived from the Human Prion Protein is Redox-​Active at Physiological pH.  Inorg. Chem. 2007, 46, 710-719.
  • Neupane, K.P.; Shearer, J.  The Influence of Amine​/Amide versus Bisamide Coordination in Nickel Superoxide Dismutase.  Inorg. Chem. 2006, 45, 10552-10566.
  • Shearer, J.; Zhao, N.  [Me4N]​(NiII(BEAAM)​)​:  A Synthetic Model for Nickel Superoxide Dismutase That Contains Ni in a Mixed Amine​/Amide Coordination Environment.  Inorg. Chem. 2006, 45, 9637-9639.
  • Frost, B.J.; Bautista, C.M.; Huang, R.; Shearer, J.  Manganese Complexes of 1,​3,​5-​Triaza-​7-​phosphaadamantane (PTA)​:  The First Nitrogen-​Bound Transition-​Metal Complex of PTA.  Inorg. Chem. 2006, 45, 3481-3483.
  • Shearer, J.; Long, L.M.  A Nickel Superoxide Dismutase Maquette That Reproduces the Spectroscopic and Functional Properties of the Metalloenzyme.  Inorg. Chem. 2006, 45, 2358-2360.
  • Frost, B.J.; Miller, S.B.; Rove, K.O.; Pearson, D.M.; Korinek, J.D.; Harkreader, J.L.; Mebi, C.A.; Shearer, J.  Synthesis, characterization, and crystal structure of a quadruply bonded dimolybdenum(II) complex containing the water-​soluble phosphine 1,​3,​5-​triaza-​7-​phosphaadamantane (PTA).  Inorg. Chim. Acta 2006, 359, 283-288.