Publication Date
2017
School
School of Health Sciences
Major
Biochemistry and Molecular Biology
Keywords
Dehaloperoxidase, Hemoglobin, Peroxidase, Peroxygenase, Heme, Oxidation
Recommended Citation
Fehr, Travis, "A pH Dependant Switch in DHP Oxidation Mechanism" (2017). Senior Honors Theses. 725.
https://digitalcommons.liberty.edu/honors/725
Abstract
Dehaloperoxidase (DHP) is a multifunctional enzyme found in Amphitrite ornata, a sediment-dwelling marine worm. This enzyme possess the structure of a traditional hemoglobin enzyme and serves as the primary oxygen carrier in A. ornata; however, it also possesses peroxidase and peroxygenase capabilities. These secondary oxidative functions provide a remarkable ability for A. ornata to resist the effects of toxic metabolites secreted by other organisms that cohabit its benthic ecosystem. This study will analyze the novel catalytic switching between peroxygenase and peroxidase oxidation mechanisms employed by DHP in response to pH changes.
