Spectroscopic analysis and dynamics of ligand binding to bacterial oxidases

The aerobic respiratory chain of Escherichia coli contains two terminal oxidases, the cytochrome bd complex and the cytochrome bo complex. Each of these enzymes functions as a ubiquinol oxidase and reduces molecular oxygen to water. Although the two enzymes perform the same function they do not show any obvious similarity between their gene sequences and therefore, their structure. This thesis addresses the differences between these two enzymes in terms of the types and number of prosthetic groups and their reactions with ligands, as determined by a variety of spectroscopic methods.

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

• Hill, John Joseph

Contributors dc:contributor

• Gennis, Robert B.

• Chemistry, Biochemistry
• Biophysics, General

Statement dc:rights

• Copyright 1994 Hill, John Joseph

Language dc:language

eng

Identifier

AAI9503214
(UMI)AAI9503214

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21061