Affiliation:
1. Department of Chemistry, East Tehran Branch, Islamic Azad University, Tehran, Iran
Abstract
The heme oxygenase (HO) enzyme is a free heme protein that binds to heme in the body. Heme acts as both a cofactor and a substrate in this enzyme. The catabolism of heme into biliverdin, monoxide carbon, and free-iron, catalyzed by heme oxygenase via three consecutive oxygenation steps, in which the heme group functions as the prosthetic group as well as the substrate. Investigations of the reactions of the peripheral substituent on the heme ring with 5-oxaporphyrin iron complexes (verdohemes) have been assumed to provide models and largely unknown for the primary step in the hydrolysis of verdohemes. In this work, a theoretical kinetics and thermodynamics study of the degradation reactions of verdohemes was performed, and calculations show that the [Formula: see text] in the hydrolysis of verdohemes with non-peripheral substituents is more negative than hydrolysis of verdohemes with peripheral substituents. In other words, the hydrolysis of verdohemes with non-peripheral substituents is more energy-efficient than verdohemes with a peripheral substituents. Equilibrium constant calculations show that hydrolysis of verdohemes with non-peripheral substituents is much faster than that of verdohemes with peripheral substituents, which is due to a more convenient nucleophilic attack on the cationic ring than the anionic ring. To acquire a good molecular understanding, peripheral substituent effects on the hydrolysis of verdoheme’s inhibitory role was studied using the DFT method.
Publisher
World Scientific Pub Co Pte Lt