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Molybdenum Cofactor Insertion in Escherichia coli Dimethyl Sulfoxide Reductase Open Access


Other title
DMSO reductase
FS0 cluster
Molybdenum Cofactor
Type of item
Degree grantor
University of Alberta
Author or creator
Tang, Huipo
Supervisor and department
Weiner, Joel H. (Biochemistry)
Examining committee member and department
Lemire, Bernard (Biochemistry)
Lemieux, Joanne (Biochemistry)
Nargang, Frank (Biological Sciences)
Fahlman, Richard (Biochemistry)
Department of Biochemistry

Date accepted
Graduation date
Master of Science
Degree level
Molybdenum is a metal present in all forms of life. Most commonly, it forms the molybdenum cofactor (Moco) in the active site of molybdoenzymes. In bacteria, dimethyl sulfoxide (DMSO) reductase is a molybdoenzyme that is part of the anaerobic respiratory chain. E. coli DMSO reductase (DmsABC) belongs to a family called the complex iron-sulfur molybdeoenzymes, which contain iron-sulfur clusters to transfer electrons through the enzyme. In E. coli nitrate reductase A, another member of this family, there is a [4Fe-4S] cluster called FS0 that also plays a role in enzyme maturation. In this thesis, DmsABC is used as a model system to explore the interplay between the FS0 cluster assembly and Moco insertion. This is achieved by generating site-directed mutations in the FS0-coordinating sequence and evaluation of effects of these mutations on assemblies of FS0 and Moco in vivo complementation and in vitro biochemical, enzymology and spectroscopic assays.
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 these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before 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
Tang H., Rothery R. A., Voss J. E. and Weiner J.H. (2011) The Journal of Biological Chemistry 286: 15147-15154.

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