Structural and Functional Studies of the Cytochrome D Oxidase Complex of Escherichia Coli

The cytochrome d oxidase complex is one of two terminal quinol oxidase complexes of Escherichia coli. The heterodimeric complex contains three heme prosthetic groups, $b\sb{558}, b\sb{595},$ and d. Two histidines, His19 and His186, in subunit I are essential for retaining the heme groups. His19 was proposed to be an axial ligand to either $b\sb{595}$ or d, and His186 was postulated to be a ligand to low spin $b\sb{558}.$

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

• Zuberi, Tamma Marie

Contributors dc:contributor

• Gennis, Robert

• Biology, Molecular
• Biophysics, General

Identifier

(UMI)AAI9329212

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/72361