Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by genetic methods

The cytochrome d terminal oxidase is one of two terminal oxidases in the aerobic respiratory chain of E. coli. The topology of the two subunits of the complex were examined by the use of alkaline phosphatase gene fusions, and models proposed. The expression and assembly of the subunits was also examined. It was found that subunit II of the complex can be expressed independently of subunit I and associates with the cytoplasmic membrane. It does not appear to have any of the cytochrome components associated with it under these conditions. The plasmid expressing subunit II complements another plasmid expressing subunit I, restoring oxidase activity. The incorporation of the $b\sb{595}$ and $d$ cytochrome components requires the association of the two subunits. It has also been confirmed that the expression of the cytochrome $d$ complex is not regulated by the presence or absence of heme. A model for the assembly of the complex has been proposed.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry, Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Newton, Gail Ann

Contributors dc:contributor

• Gennis, Robert B.

• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1990 Newton, Gail Ann

Language dc:language

eng

Identifier

AAI9026280
(UMI)AAI9026280

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/23829