Department or Program
Biological Chemistry
Abstract
Structural and mechanistic insight into the non-heme diiron proteins will likely lead to advances in bioremediation, biomimetic catalysis, and directed protein engineering. Iron metalloproteins are capable of catalyzing a wide variety of chemical reactions. The non-heme diiron proteins represent a distinct class of metalloproteins able to activate molecular oxygen and perform key reactions in biological systems including alkane C-H bond oxidation, alkene epoxidation, and lipid desaturation. This thesis focuses on the structural and mechanistic characterization of the integral membrane non-heme diiron protein, alkane monooxygenase (AlkB), from the oil-degrading bacterium, Alcanivorax borkumensis. The purification of active AlkB was optimized and crystallization methodology was developed in an attempt at complete structural resolution. In combination with work on the other diiron proteins, it may be possible to develop a coherent model with which to explore the unique chemistry of this metal-binding motif.
Level of Access
Open Access
First Advisor
Austin, Rachel
Date of Graduation
5-2013
Degree Name
Bachelor of Science
Recommended Citation
Born, David Allan, "Structural and mechanistic characterization of the integral membrane non-heme diiron protein, alkane monooxygenase, from the oil-degrading bacterium Alcanivorax borkumensis" (2013). Honors Theses. 72.
https://scarab.bates.edu/honorstheses/72
Number of Pages
110
Components of Thesis
1 pdf file
Embargoed
Open Access
Available to all.