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Mississippi State University

1. Wilson, David L. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.

Degree: PhD, Chemistry, 2015, Mississippi State University

This report details the activities and inhibition of metal-substituted human carbonic anhydrase II (M-HCA-II). The traditional activities (hydrolysis of CO2 and <I>para</I>-nitrophenol acetate) in addition to new activities (oxidation of 2-aminophenol, disproportionation of H2O2, and disproportionation of superoxide) were investigated. Values reported for the relative hydrolytic activities of M-HCA-IIs are reported here for the first time, ranging from 47.5 % (plus or minus 0.6) to 86 % (plus or minus 4) for the hydrolysis of CO2 and from 0.299 % (plus or minus 0.012) to 4.72 % (plus or minus 0.015) for the hydrolysis of <I>para</I>-nitrophenol acetate. With respect to new activities, only the oxidation of 2-aminophenol was observed. Turnover was observed for Fe-HCA-II (kcat/KM = 3.6 plus or minus 1.3 mM-1 s-1) and Cu-HCA-II (kcat/KM = 8 plus or minus 2 mM-1 s-1). Inhibition of Zn-, (di-substituted) Cu2-, and Cu/Zn-HCA-II hydrolysis of CO2 and <I>para</I>-nitrophenol acetate by sulfanilamide, coumarin, and <I>ortho</I>-coumaric acid were investigated. Sulfanilamide was shown to inhibit: Zn-HCA-II, Cu2-HCA-II, and Cu/Zn-HCA-II - (with CO2) KM = 8.9 plus or minus 1.1 microM, 11 plus or minus 2 microM, 8.8 plus or minus 1.4 microM and (with p-nitrophenyl acetate) KM = 8.4 plus or minus 1.0 microM, (none), 8.4 plus or minus 1.4 microM, respectively. No inhibition was observed for coumarin or <I>ortho</I>-coumaric acid or its derivatives for any CAs studied. Advisors/Committee Members: Joseph P. Emerson (chair), Edwin A. Lewis (committee member), Todd E. Mlsna (committee member), Nicholas C. Fitzkee (committee member), Debbie J. Beard (committee member).

Subjects/Keywords: human carbonic anhydrase II; HCA-II; metal-substitution; copper; cobalt; manganese; iron; nickel; sulfanilamide; coumarin; kinetics; 2-aminophenol; catalase; superoxide dismutase; peroxidase

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Wilson, D. L. (2015). Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. (Doctoral Dissertation). Mississippi State University. Retrieved from http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;

Chicago Manual of Style (16th Edition):

Wilson, David L. “Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.” 2015. Doctoral Dissertation, Mississippi State University. Accessed April 16, 2021. http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;.

MLA Handbook (7th Edition):

Wilson, David L. “Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition.” 2015. Web. 16 Apr 2021.

Vancouver:

Wilson DL. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. [Internet] [Doctoral dissertation]. Mississippi State University; 2015. [cited 2021 Apr 16]. Available from: http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;.

Council of Science Editors:

Wilson DL. Human carbonic anhydrase II: preparation, metal-substitution, activity, and inhibition. [Doctoral Dissertation]. Mississippi State University; 2015. Available from: http://sun.library.msstate.edu/ETD-db/theses/available/etd-06222015-164959/ ;

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