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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. <http://www.rcsb.org/pdb/101/motm.do?momID=49>.
ii Ophardt, Charles E. "Oxygen Transport." Oxygen Transport. Elmhurst College, 2003. Web. 17 Mar.
iii 3 Harper College. "Blood Buffer - Normal Bodily Function." Blood Buffer - Normal Bodily Function.
N.p., n.d. Web. 17 Mar. 2013. <http://www.harpercollege.edu/tmps/chm/100/dgodambe/thedisk/bloodbuf/zback2.htm>.
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.
vi Wothington Biochemical Company. "Carbonic Anhydrase." - Worthington Enzyme Manual. N.p.,
2013. Web. 17 Mar. 2013. <http://www.worthington-biochem.com/ca/default.html>.
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.
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,
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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