The Purification and Characterization of The Cytochrome D Containing Terminal Oxidase of Escherichia Coli (Bioenergetics, Membranes, Ultracentrifugation)

The cytochrome d-containing terminal oxidase of Escherichia coli has been purified to at least 90% of homogeneity, judging from the Coomassie blue staining of SDS-polyacrylamide gels. These gels showed that the cytochrome contained two types of subunits with molecular weights of 57,000 Daltons and 43,000 Daltons from the analysis of a Ferguson plot, or 53,000 Daltons and 28,000 Daltons from the analysis of 12.5% gels. Reduced minus oxidized spectra of the cytochrome showed that cytochromes a(,1), b(,558) and d are present. Protoheme IX and heme d were the only prosthetic groups found in the complex, and iron was the only metal. This suggests that cythochrome a(,1) contains protoheme IX as a prosthetic group. Heme d is probably the site of oxygen binding, since both carbon monoxide and oxygen perturb its spectrum.

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

2014

Author dc:creator

• Miller, Michael Joseph

• Chemistry, Biochemistry

Identifier

(UMI)AAI8502248

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70538