The Utilization of Metalloporphyrins as Mechanistic Probes of the Active Site of Heme Proteins
type: CreativeWork
description: 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.
abstract: 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.
author: Reinert, Thomas Joseph
keywords: Chemistry, Inorganic
date published: 2014-12-15T23:19:09Z
date modified: 2026-07-22T22:26:02Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/70393