Cytochrome AA(3) from Rhodobacter sphaeroides: Affinity purification and biophysical characterization of site-directed mutants

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Mitchell, David Michael

Contributors dc:contributor

• Gennis, Robert B.

• Chemistry, Biochemistry
• Biophysics, General

Statement dc:rights

• Copyright 1996 Mitchell, David Michael

Language dc:language

eng

Identifier

9780591198393
AAI9712382
(UMI)AAI9712382

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22548