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.
University of Illinois - Urbana-Champaign
Networked Digital Library of Theses and Dissertations
University of Illinois at Urbana-Champaign