Download the full-sized PDF of The function of the electron transfer chain in Escherichia coli succinate dehydrogenaseDownload the full-sized PDF



Permanent link (DOI):


Export to: EndNote  |  Zotero  |  Mendeley


This file is in the following communities:

Graduate Studies and Research, Faculty of


This file is in the following collections:

Theses and Dissertations

The function of the electron transfer chain in Escherichia coli succinate dehydrogenase Open Access


Other title
reactive oxygen species
electron transfer chain
quinone binding site
electron paramagnetic resonance
iron-sulfur cluster
Escherichia coli
complex II
succinate dehydrogenase
electron tunneling
Type of item
Degree grantor
University of Alberta
Author or creator
Tran, Quang
Supervisor and department
Weiner, Joel (Biochemistry)
Examining committee member and department
Lemire, Bernard (Biochemistry)
Iverson, Tina (Pharmacology)
Glover, Mark (Biochemistry)
Nargang, Frank (Biological Sciences)
Department of Biochemistry

Date accepted
Graduation date
Doctor of Philosophy
Degree level
Complex II, or succinate dehydrogenase, is a vital component of aerobic life. Its function is critical for both the tricarboxylic acid cycle and the mitochondrial respiratory chain since it catalyzes the oxidation of succinate to fumarate, liberating two electrons that feed into the lipid-soluble quinone pool. Despite over 50 years of research, and the fact that it is the simplest of all the mitochondrial respiratory chain complexes, there is still much to learn regarding the catalytic mechanism of complex II. In recent years, there has been a renewed interest in this enzyme, due to its central role in a subset of human cancers, hereditary paraganglioma and pheochromocytoma. For my research, I chose Escherichia coli succinate dehydrogenase as the model system due to its innumerable similarities to mitochondrial complex II. In chapter two, I examine key residues that enable succinate dehydrogenase to interact with its quinone substrate. Chapters three and four focus on the function of the single b-type heme in the enzyme, and its potential role, or lack thereof, in enzyme catalysis and suppression of reactive oxygen species production. In chapter five, microsecond freeze-hyperquench experiments are utiilized to empirically quantify electron transfer rates through the succinate dehydrogenase iron-sulfur cluster relay, and examine the control that endergonic electron tunneling steps exert on those rates.
License granted by Quang Tran ( on 2011-08-31T21:55:57Z (GMT): Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of the above terms. The author reserves all other publication and other rights in association with the copyright in the thesis, and except as herein provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
Citation for previous publication

File Details

Date Uploaded
Date Modified
Audit Status
Audits have not yet been run on this file.
File format: pdf (Portable Document Format)
Mime type: application/pdf
File size: 28840265
Last modified: 2015:10:12 12:06:05-06:00
Filename: Tran Thesis.pdf
Original checksum: b3fe6aa55bdedc552bd5c9bbe4cafe4b
Well formed: true
Valid: true
Status message: File header gives version as 1.4, but catalog dictionary gives version as 1.3
File title: Thesis - All text_final
File author: Quang Tran
Page count: 229
Activity of users you follow
User Activity Date