University of Illinois Urbana-Champaign

Cytochrome AA(3) From Rhodobacter Sphaeroides: Affinity Purification and Biophysical Characterization of Site-Directed Mutants

Mitchell, David Michael

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Description

Title
Cytochrome AA(3) From Rhodobacter Sphaeroides: Affinity Purification and Biophysical Characterization of Site-Directed Mutants
Author(s)
Mitchell, David Michael
Issue Date
1996
Doctoral Committee Chair(s)
Gennis, Robert B.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biophysics, General
Language
eng
Abstract
Cytochrome c oxidase of R. sphaeroides has been purified using affinity methods and studied using site-directed mutagenesis coupled with a wide variety of biophysical characterization methods. Two methods of affinity purification were developed. Site-directed mutants were constructed in regions of the protein which were predicted to be important for enzyme function by sequence analysis. Methods ranging from visible and vibrational spectroscopy to rapid kinetic measurements of electron and proton transfers were used to probe the various effects of these mutants on the structure and function of the enzyme. Results were interpreted, when possible, in terms of possible redox-linked proton pumping mechanisms, or alternatively, on a purely phenomenological basis.
Graduation Semester
1996
Type of Resource
text
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http://hdl.handle.net/2142/84873

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