Molecular genetic studies of the cytochrome o terminal oxidase complex in Escherichia coli

The cytochrome $o$ terminal oxidase complex is a component of aerobic respiratory chain of Escherichia coli. This enzyme catalyzes the oxidation of ubiquinol-8 to ubiquinone-8 within the cytoplasmic membrane and the concomitant reduction of O$\sb2$ to H$\sb2$O. Cytochrome $o$ oxidase has been purified and shown to contain four subunits on SDS-PAGE gels. The cloning of the $cyo$ operon makes it possible to address a number of problems concerning the structure and function of the cytochrome $o$ oxidase complex. Detailed analysis of this operon will enable us to identify the subunit compositions, the locations of the hemes, etc.

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

• Chepuri, Visala

Contributors dc:contributor

• Gennis, Robert B.

• Biology, Molecular
• Biology, Genetics
• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1990 Chepuri, Visala

Language dc:language

eng

Identifier

AAI9026156
(UMI)AAI9026156

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21143