chem research paper 1

Is seen that ion substitution for zinc is a favorable

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Unformatted text preview: ate ligand from atmospheric CO2 as a model shown in Figure 8. Therefore it can be seen that parallels between the metal bound complex and the new complex that this ligand may induce more favorable electron movement and carbonate formation. It is seen that ion substitution for zinc is a favorable attribute of the zinc carbonic anhydrase. Although there is a lack of specifics for substitution productivity, there is enough supporting evidence to confirm that enzyme activity is still present and applicable outside of solely experimental conditions. The discussion of carbonic anhydrase stems from its consistency to perform its function in a variety of situations like differences in polarity and active site confirmations, and even replacement of its main metal ion, zinc. The greatest ability of the carbonic anhydrase is its unknown potential with ion substitutions and being able to function at a similar level or higher level. This leads to many areas of future research regarding experimental ion substitutions, as well as a closer examination of recognized and potential novel zinc substitutions occurring across nature. In conclusion, zinc carbonic anhydrase is an enzyme that has many conformations that are equally as productive due to the consistency of the proton transfer in the enzyme mechanisms and the structural similarities. i Dutta, Shuchismita, and David Goodsell. "Carbonic Anhydrase." RCSB PDB-101. RCSB Protein Data Bank, Jan. 2004. Web. 17 Mar. 2013. <>. ii Ophardt, Charles E. "Oxygen Transport." Oxygen Transport. Elmhurst College, 2003. Web. 17 Mar. 2013. iii 3 Harper College. "Blood Buffer - Normal Bodily Function." Blood Buffer - Normal Bodily Function. N.p., n.d. Web. 17 Mar. 2013. <>. iv Tymoczko, J. L., and L. Stryer. "Making a Fast Reaction Faster: Carbonic Anhydrase."Biochemistry. By J. M. Berg. 5th ed. New York: W.H. Freeman, 2002. N. pag. NCBI. Web. 17 Mar. 2013. <>. v Sigma-Aldrich. "Carbonic Anhydrase." Sigma-Aldrich. Sigma-Aldrich, n.d. Web. 17 Mar. 2013. < TablePage=16192499>. vi Wothington Biochemical Company. "Carbonic Anhydrase." - Worthington Enzyme Manual. N.p., 2013. Web. 17 Mar. 2013. <>. vii Elder, Ileana. "Kinetic and Structural Studies on the Activation of the Protein Transfer in Catalysis by Carbonic Anhydrase." Diss. University of Florida, 2004. Web. 17 Mar. 2013, 11-26. viii Lesnichin, Stepan B. "Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR." Journal of the American Chemical Society (n.d.): n. pag. Print, 1-6. ix Avvaru, Balendu Sankara, Chae Un Kim, and David N. Silverman. "A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II†,‡."Biochemistry 49 (2010): 249-51. Web. 17 Mar. 2013,1. x Satcher, J. H., and S. E. Baker. "Modeling, Synthesis and Characterization of Zinc Containing Carbonic Anhydrase Active Site Mimics." Energy Procedia 4 (2011): 2090-095. Web. 17 Mar. 2013, 2091-94. xi Banci, L., L. B. Dugad, G. N. La Mar, K. A. Kearing, C. Luchinat, and R. Pierattelli. "1H Nuclear Magnetic Resonance Investigation of Cobalt(II) Substituted Carbonic Anhydrase." Biophysical Journal 63.2 (1992): 530-43. Online,530-37. xii Bebout, Deborah C, Wei Lei, Steven M. Berry, William P. Kaplan, Malia S. Hain, and John C. Postma. "Carbonate Templated Self-Assembly of an Alkylthiolate Bridged Cadmium Macrocycle." Inorganic Chemistry (2012): n. pag. Print, 1-3. xiii Park, Haewon. "Cadmium Carbonic Anhydrase of Marine Diatoms: Diversity and Expression." Diss. Princeton University, 2008. Cadmium Carbonic Anhydrase of Marine Diatoms: Diversity and Expression. Jan. 2008. Web. 17 Mar. 2013. xiv Xu, Yan, Liang Feng, and Philip D. Jeffery. "Structure and Metal Exchange in the Cadmium Carbonic Anhydrase of Marine Diatoms." Nature (2008): 56-62. Web. 17 Mar. 2013, 56-60....
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This note was uploaded on 10/01/2013 for the course CHEM 305 taught by Professor Mcnamara during the Spring '13 term at William & Mary.

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