Molybdenum Cofactor Insertion in Escherichia coli Dimethyl Sulfoxide Reductase

  • Author / Creator
    Tang, Huipo
  • 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.

  • Subjects / Keywords
  • Graduation date
  • Type of Item
  • Degree
    Master of Science
  • DOI
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
  • Language
  • Institution
    University of Alberta
  • Degree level
  • Department
    • Department of Biochemistry
  • Supervisor / co-supervisor and their department(s)
    • Weiner, Joel H. (Biochemistry)
  • Examining committee members and their departments
    • Nargang, Frank (Biological Sciences)
    • Fahlman, Richard (Biochemistry)
    • Lemieux, Joanne (Biochemistry)
    • Lemire, Bernard (Biochemistry)