Analysis of heme-copper ligation, quinol activity, and ligand binding kinetics of cytochrome BO(3) quinol oxidase from E. coli

Structural and functional properties of wild type and mutant forms of cytochrome $bo\sb3$ quinol oxidase from E.coli were examined. Structural properties of subunit II were addressed with the restoration of the putative Cu$\sb{\rm A}$ ligands and construction of a chimeric E.coli/R.sphaeroides subunit II. Functional properties of subunit II were interpreted with azido-Q labelling studies. General properties of the wild type enzyme were interpreted with respect to heme content, ubiquinol content, absolute absorption spectra, ligand bound absorption spectra, and ligand binding kinetics. Structural and functional perterbations by the mutation of conserved residues were determined with ligand binding kinetics. Finally, construction and characterization of histidine tagged subunits I, II, and III was described.

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

• Rumbley, Jon Nolan

Contributors dc:contributor

• Gennis, Robert B.

• Chemistry, Biochemistry
• Chemistry, Physical

Statement dc:rights

• Copyright 1995 Rumbley, Jon Nolan

Language dc:language

eng

Identifier

AAI9624477
(UMI)AAI9624477

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/20492