The Utilization of Metalloporphyrins as Mechanistic Probes of the Active Site of Heme Proteins

Iron protoporphyrin-IX is a ubiquitous active site in biological systems. It provides the redox couple for electron transport, facilitates the insertion of an oxygen atom into an organic substrate, and also serves as the binding site for dioxygen in O$\sb2$ transport/storage hemoproteins. In the latter, one observes a range of 10$\sp5$ in O$\sb2$ affinities among heme proteins, discrimination in binding O$\sb2$ vs. CO, and cooperative ligand binding observed in hemoglobin.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Reinert, Thomas Joseph

• Chemistry, Inorganic

Identifier

(UMI)AAI8803173

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70393