Undergraduate Programs

Bio

Teaching Interests

Dr. Stoj teaches biochemistry and general chemistry.

Research Interests

Dr. Stoj is fascinated by the structure and function of proteins involved in the maintenance of metal ion homeostasis in biology, specifically as they relate to various neurodegenerative disease states. The aims of his research group are to better understand the complex nature of metal ion cofactors in biological health and disease states.  The critical requirement for metal ions in biology has been known for many years and is typified by the red pigment of human blood as a result of oxygenated iron-loaded hemoglobin.  Currently, altered metal ion homeostasis is considered a causative agent of many disease states including those of neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Amyotrophic Lateral Sclerosis, also known as Lou Gehrig’s disease. We employ current biochemical and biophysical research tools to examine metal ion relationships to cardiovascular and neurodegenerative disorders, anemia, diabetes, as well as probe the mechanisms by which proteins and enzymes uptake, store, and mobilize metal ions. 

Education

• Ph.D. Biochemistry (2006), State University of New York at Buffalo
• B.S. Chemistry (ACS) and Biology minor (2000), Plattsburgh State University of New York

Professional Experience

• Chair, Dept. of Biochemistry, Chemistry and Physics, Niagara University, 2012-present
• Associate Professor, Dept. of Biochemistry, Chemistry and Physics, Niagara University, 2012-present
• Assistant Professor, Dept. of Biochemistry, Chemistry and Physics, Niagara University, 2006-2012

Publications

11. Augustine, T. J., Kragh, M. E., Sarangi, R., Fujii, S., Liboiron, B. D., Stoj, C. S., Kosman, D. J., Hodgson, K. O., Hedman, B., and Solomon, E. I.  “Spectroscopic studies of perturbed T1 Cu sites in the multicopper oxidases Saccharomyces cerevisiae Fet3p and Rhus vernicifera Laccase: allosteric coupling between the T1 and trinuclear Cu sites” Biochemistry, 2008, 47(7), 2036-2045.

10. Augustine, T. J., Quintanar, L., Stoj, C. S., Kosman D. J., and Solomon E. I. “Spectroscopic and kinetic studies of perturbed trinuclear copper clusters: The role of protons in reductive cleavage of the O-O bond in the multicopper oxidase Fet3p” Journal of the American Chemical Society, 2007, 129(43), 13118-13126.

9. Quintanar, Lilliana; Stoj, Christopher; Taylor, Alexander B.; Hart, P. John.; Kosman, Daniel J.; and Solomon, Edward. I “Shall we dance? How a multicopper oxidase chooses its electron transfer partner” Accounts of Chemical Research, 2007, 40(6), 445–452.

8. Stoj, Christopher S.; Augustine, Anthony J.; Solomon, Edward I.; Kosman, Daniel J. “Structure-Function Analysis of the Cuprous Oxidase Activity in Fet3p from Saccharomyces cerevisiae” Journal of Biological Chemistry, 2007, 282(11), 7862-7868.

7. Stoj, Christopher S.; Augustine, Anthony J.; Zeigler, Lynn; Solomon, Edward I.; Kosman, Daniel J. “Structural Basis of the Ferrous Iron Specificity of the Yeast Ferroxidase, Fet3p.” Biochemistry, 2006, 45(42), 12741-12749.

Prior to joining NU

6. Kwok, E. Y.; Stoj, C. S.; Severance, S.; Kosman, D. J. “An engineered bifunctional high affinity iron uptake protein in the yeast plasma membrane” Journal of Inorganic Biochemistry, 2006, 100(5-6), 1053-1060.

5. Taylor, Alexander B.; Stoj, Christopher S.; Ziegler, Lynn; Kosman, Daniel J.; Hart, P. John. “The copper-iron connection in biology: Structure of the metallo-oxidase Fet3p” Proceedings of the National Academy of Sciences of the United States of America, 2005, 102(43), 15459-15464.

4. Stoj, Christopher S. and Kosman, D. J. “Copper Oxidases” in Encyclopedia of Inorganic Chemistry, 2nd Ed., R. B. King, editor, John Wiley, 2005.

3. Quintanar, Liliana; Stoj, Christopher; Wang, Tzu-Pin; Kosman, Daniel J.; Solomon, Edward I. “Role of Aspartate 94 in the Decay of the Peroxide Intermediate in the Multicopper Oxidase Fet3p” Biochemistry, 2005,  44(16), 6081-6091.

2. Shi, Xiaoli†; Stoj, Christopher †; Romeo, Annette; Kosman, Daniel J.; Zhu, Zhiwu. “Fre1p Cu2+ Reduction and Fet3p Cu1+ Oxidation Modulate Copper Toxicity in Saccharomyces cerevisiae” Journal of Biological Chemistry, 2003, 278(50), 50309-50315. († Contributed equally to the research described in this paper.)

1. Stoj, Christopher and Kosman, Daniel J. “Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function.” FEBS Letters, 2003, 554(3), 422-426.