Long-range electron transfer in cobalt-labeled cytochrome c

In order to investigate the relationship between intramolecular electron transfer kinetics and redox site separation distance, a semisynthetic two-site donor/acceptor system, in which the distance between redox sites was fixed and known, was prepared. The approach taken involved attachment of the macrocyclic cage complex (Co(diAMsar)) $\sp{3+}$ to various sites on the surface of horse heart cytochrome c. In this way, a second redox site, in addition to the heme, was introduced. Labelling of the protein at several surface sites, allowed several donor/acceptor distances to be evaluated within the same protein system.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry, Analytical

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Conrad, David William

Contributors dc:contributor

• Faulkner, Larry R.
• Scott, R.A.

• Chemistry, Analytical
• Chemistry, Inorganic

Statement dc:rights

• Copyright 1990 Conrad, David William

Language dc:language

eng

Identifier

AAI9021665
(UMI)AAI9021665

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21462