Prof. Shearer was born in Maryland and attended the University of Maryland, College Park where he obtained a B.S. in Biochemistry and Cell and Molecular Biology. It was during this time that he developed an interest in chemistry while performing research in the laboratory of Prof. Steven Rokita. Following studies at the University of Maryland, Prof. Shearer pursued graduate work at the University of Washington in Seattle under Prof. Julie Kovacs as an EPA predoctoral fellow. He primarily investigated the reactivity and bonding of thiolate ligated transition metal complexes with relevance to metalloenzymes such as nitrile hydratase and superoxide reductase. It was during graduate studies, under the guidance of Prof. Robert Scarrow (Haverford College), that he gained a fascination with X-ray spectroscopic methods. After his graduate work he moved to Johns Hopkins University as an NIH postdoctoral fellow where he performed research under the mentorship of Prof. Kenneth Karlin. As a postdoc, Prof. Shearer investigated the mechanism by-which copper dioxygen complexes effect substrate oxidations. Prof. Shearer then started his independent career at the University of Nevada, Reno, where over the course of 14 years he established a research program in bioinorganic and physical inorganic chemistry. Prof. Shearer then moved to Trinity in 2018.
Prof. Shearer’s current research interests center on understanding how the structure and bonding of biologically relevant late first row transition metal compounds influence their reactivity. He is especially interested in understanding how the structure of cysteinate-ligated nickel-containing metalloenzymes contribute to their function, protein evolutionary mechanisms, and atypical bonding schemes in transition metal complexes. To these ends his research group prepares and investigates small metallopeptides, metalloproteins, and transition metal complexes. Owing to the highly multidisciplinary nature of this research, students in his group are exposed to a large array of chemical techniques and methods including: peptide and small molecule synthesis, spectroscopy (UV-vis/NIR, (M)CD, Raman and X-ray absorption/emission spectroscopies), and computational methods.
Postdoc in Chemistry, Johns Hopkins University
Ph.D. in Inorganic Chemistry, University of Washington
B.S. in Biochemistry and Cell & Molecular Biology (double major), University of Maryland, College Park
B. J. Cook, G. N. Di Francesco, R. B. Ferreira, J. T. Lukens, K. E. Silberstein, B. C. Keegan, V. J. Catalano, K. M. Lancaster, J. Shearer, L. J. Murray “Chalcogen Impact on Covalency within Molecular [Cu3(µ3-E)] 3+ Clusters (E = O, S, Se): A Synthetic, Spectroscopic, and Computational Study” 2018, Inorg. Chem. 2018, 57, 11382-11392 (DOI: 10.1021/acs.inorgchem.8b01000)
B. Wang, Y.-M. Lee, W. Tcho, S. Tussupbayev, S.-T. Kim, Y. Kim, S. Seo, K.-B. Cho, Y. Dede, T. Ogura, S. H. Kim, T. Ohta, M.-H. Baik, K. Ray, B. C. Keegan, J. Shearer and W. Nam “Photocatalytic Generation of a Mononuclear Nonheme Cobalt(IV)-oxo Complex: Synthesis, Spectroscopic Characterization, and Reactivity Studies.” Nature Commun. 2017, 8, Article Number: 14839 (DOI: 10.1038/ncomms14839)
J. Shearer, J.C. Schmitt and J.S. Clewett “Adiabiticity of the Proton Coupled Electron Transfer Process in the Reduction of Superoxide by a Nickel Containing Superoxide Dismutase Metallopeptide Based Mimic.” J. Phys. Chem. B 2015, 119, 5453-5461. (DOI: 10.1021/acs.jpcb.5b02640)
J. Shearer, K. L. Peck, J.C. Schmitt, K. P. Neupane, “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 (DOI: 10.1021/ja5079514)
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)