Yelu Shi
Assistant Professor
College of Science and Technology
- Office: GEH C415
- Email: yshi@kean.edu

Education
B.S. in Polymer Science and Engineering
University of Science and Technology of China, Hefei
M.S. in Chemistry
Stevens Institute of Technology, Hoboken
Ph.D. in Chemistry
Stevens Institute of Technology, Hoboken
Courses teaching in WKU
Chemistry I (with Laboratory)
Biography
Dr. Yelu Shi found her research interest in the structural and mechanistic investigation of metalloprotein reactions, and how such reactions are connected with human disease, public health, and environmental science. Her academic education in chemistry and biochemistry has built the foundation for her interest, and her research experience in both applied chemistry and theoretical biochemistry has enabled her to deeply, systematically, and comprehensively address significant research problems in this area.
Dr. Shi worked on the synthesis and modifications of nanomaterials and their application in drug delivery during her Master’s in the U.S. Later on, she found her passion for theoretical chemistry and joined the High Accuracy Computational Chemistry Laboratory at Stevens. Dr. Shi focused on theoretical studies of metal-mediated formation, conversion, and detection of the biological molecule HNO. Meanwhile, she has cooperated with mass spectroscopy and bioinorganic chemistry researchers, and these collaborations have resulted in several publications on top peer-reviewed journals.
After two years of postdoctoral experience on the large-scaled quantum mechanics / molecular mechanics (QM/MM) method simulation, Dr. Shi joined Wenzhou-Kean University as a faculty member.
Academic Experience:
Adjunct Lecturer, January 2020-May 2020
Stevens Institute of Technology, NJ, USA
Course: Quantum Chemistry, Theoretical Chemistry
Postdoctoral, July 2018-May 2020
Stevens Institute of Technology, NJ, USA
Research interests
My research interests revolve around the mechanistic investigation of transition metal complexes and their catalytic application in organic, organometallic, biological, and environmental chemistry. Specifically, my primary focus is on earth-abundant first-row transition metal complexes and their catalytic mechanisms of C-H/N-H functionalization, nitrile hydration, and hydrogen borrowing.
Selected Publications/scholarly and creative work
- Selvan D, Shi Y, Prasad P, Crane S, Zhang Y*, Chakraborty S*. Dalton Trans., 49, 1928-1934 (2020). The Oxygen Reactivity of an Artificial Hydrogenase Designed in a Reengineered Copper Storage Protein.
- Selvan D, Prasad P, Farquhar ER, Shi Y, Crane S, Zhang Y, Chakraborty S*. ACS Catal., 9, 5847-5859 (2019). Redesign of a Copper Storage Protein into an Artificial Hydrogenase.
- Shi Y, Zhang Y*. Angew. Chem. Int. Ed., 57, 16654-16658 (2018). Mechanisms of HNO Reactions with Ferric Heme Proteins.
- Bhagi-Damodaran A, Reed J, Zhu Q, Shi Y, Hosseinzadeh P, Sandoval BA, Harden KA, Wang, S, Sponholtz MR, Dwaraknath S, Zhang Y*, Moënne-Loccoz P, Lu Y. Proc. Natl. Acad. Sci. U. S. A., 115, 6195-6200 (2018). Heme Redox Potential Holds Key to Reactivity Differences Between Nitric Oxide Reductase and Heme-Copper Oxidase.
- Reed J, Shi Y, Zhu Q, Chakraborty S, Mirts EN, Petrik ID, Bhagi-Damodaran A, Ross M, Moënne-Loccoz P, Zhang Y*, Lu Y. J. Am. Chem. Soc., 139, 12209-12218 (2017). Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.
- Bhagi-Damodaran A, Kahle M, Shi Y, Zhang Y*, Ӓdelroth P, Lu Y. Angew. Chem. Int. Ed., 56, 6622-6626 (2017). Insights into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-Based Functional Oxidase.
- Khade RL, Yang Y, Shi Y, Zhang Y*. Angew. Chem. Int. Ed., 55, 15058-15061 (2016). HNO Binding in Heme Proteins: Effects of Iron Oxidation State, Axial Ligand, and Protein Environment.
- Shi Y, Selin V, Wang Y, Sukhishvili SA*. Part. Part. Syst. Charact., 30, 950-957 (2013). Multiresponsive Block Copolymer-Modified “Hairy” Gold Nanoparticles for Remote Control of Interfaces.