Honors Theses
Date of Award
Spring 5-9-2024
Document Type
Undergraduate Thesis
Department
Chemistry and Biochemistry
First Advisor
Saumen Chakraborty
Second Advisor
Kensha Clark
Third Advisor
Jonah Jurss
Relational Format
Dissertation/Thesis
Abstract
Metalloenzymes perform a wide variety of reactions that are instrumental to the basic functions of life. Learning more about those enzymes–their structure, folding, active sites, and co-factors–can help to not only better understand the finer details of the chemical world, but also help provide answers and possible solutions to questions pertaining to alternative energy. Particulate Methane Monooxygenase (pMMO) is a metalloenzyme that oxidizes methane into methanol in the biological processes of some methanogenic bacteria, a valuable part of their process to obtain energy. One of its active sites, CuB, has a relatively unknown function. Heptad repeats of model enzymes have been designed using De Novo Synthesis to be able to study the reactivity of that active site. A tetramer of that enzyme, 4SCC, has been synthesized but found to be unreactive while using Cu as the metal cation. The function, reactivity, and properties of a metalloenzyme are greatly influenced by the metal cation used in the enzyme. Fe(III) and Mn(II) are widely bioavailable, especially Fe(III). Both transition metals also have access to several oxidation states with Mn having the highest number of oxidation states of any transition metal. These metals can be substituted and bound to 4SCC in hopes of finding and studying the more favorable reactivity of this “CuB” active site through oxidation and kinetic experiments.
Recommended Citation
Randall, Hannah and Upton, Russ, "Fe(III) and Mn(II) Binding De Novo Designed Peptides and Their Oxidation with H2O2" (2024). Honors Theses. 3090.
https://egrove.olemiss.edu/hon_thesis/3090
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