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Nearly half of all enzymes contain a metal ion cofactor. Divalent metal ions can be found in each of the six enzymes classes, and more often than not these metal ions play roles in directing their chemistry. Nature uses a number of strategies to match metal ions with specific proteins, including sequestration and compartmentalization. However, understanding the driving forces behind metal ion selectivity and how these metal ions influence the fidelity of biocatalytic processes remains ambiguous. The Emerson laboratory is focused on unraveling these issues. Students in the Emerson group gain experience in using a number of spectroscopic and thermodynamic tools to characterize the structure and dynamic changes associated with metal ion coordination chemistry in small molecule, peptide, and protein based systems.
He Song, Andrew C. Weirtz, Michael P. Hendrich, Edwin A. Lewis, Joseph P. Emerson, Characterizing a noncoupled dicopper center in Cu2+-substituted human carbonic anhydrase II, Journal of Biological Inorganic Chemistry, 2013 18(6), 595-598
Joseph P. Emerson, Vu H. Le, Edwin A. Lewis, Calorimetry, eLS (Encyclopedia of Life Sciences), 2012, John Wiley & Sons Ltd, http://www.els.net [doi:10.1002/9780470015902.a0003010.pub3]
He Song, David L. Wilson, Erik R. Farquhar, Edwin A. Lewis, and Joseph P. Emerson, Revisiting Zinc Binding in Human Carbonic Anhydrase, Inorganic Chemistry, 2012 51(20), 11098-105
Kate L. Henderson, Vu H. Le, Edwin A. Lewis, Joseph P. Emerson, Exploring Substrate Binding in Homoprotocatechuate 2,3-Dioxygenase using Isothermal Titration Calorimetry, Journal of Biological Inorganic Chemistry, 2012 17(7), 991-4