Date of Award
2011
Document Type
Dissertation/Thesis
Submission Date
October 2026
Thesis/Dissertation Advisor [Chair]
Kirchman, Paul A.
Abstract
Oxidative stress occurs when reactive oxygen species (ROS), such as superoxide anion (O2' —), hydroxyl radical (HO.), and hydrogen peroxide (H2O2), build up to detrimental levels in the cell, and effects of oxidative stress are associated with aging. Mitochondria are the main site of oxidative stress, most likely due to the high level of ROS produced during respiration. Mitochondrial aconitase is an enzyme involved in respiration; due to the presence of an iron-sulfur cluster in the active site, it is a target for ROS. A plasmid containing the aconitase gene to be inserted into Saccharomyces cerevisiae was designed, and will be used in the future for the pop-in pop-out method; mitochondrial aconitase will be subjected to point mutations, replacing several leucine and isoleucine amino acid residues with methionine residues near the active site and on the surface of the enzyme. The amino acid methionine has a sulfur group, which also acts as a target for ROS and could prevent inactivation of the iron-sulfur cluster of aconitase.
Recommended Citation
Batlle, Jessica, "Lowering oxidative stress with increased methionine content of mitochondrial aconitase" (2011). Harriet L Wilkes Honors College Theses 2010 - 2019. 36.
https://digitalcommons.fau.edu/etd_honors_2/36
Extent
25 p.
Identifier
FA00003557
Comments
Includes bibliography.