VIII. Substrate Specificity IX. The First Stage:-meso-Hydroxylation A. Formation of the
Activated Oxygen Species B. Substitution of H2O2 for O2 and Reducing Equivalents C …

Major advances have been made in determining the structure of heme oxygenase and the
relationship between its structure and catalytic activity. The nature of the first step in the …

Heme oxygenase catalyzes the three step-wise oxidation of hemin to α-biliverdin, via α-
meso-hydroxyhemin, verdoheme, and ferric iron–biliverdin complex. This enzyme is a …

Heme oxygenase catalyzes the regiospecific oxidation of hemin to biliverdin IXα with
concomitant liberation of CO and iron by three sequential monooxygenase reactions. The α …

The origin of the unusual regioselectivity of heme oxygenation, ie the oxidation of heme to δ-
biliverdin (70%) and β-biliverdin (30%), that is exhibited by heme oxygenase from …

Heme oxygenase is a central enzyme of heme degradation and associated carbon
monoxide biosynthesis. We have prepared the α-hydroxyheme-heme oxygenase complex …

Heme degradation through the action of heme oxygenase (HO) is unusual in that it utilizes
heme as both a substrate and cofactor for its own degradation. HO catalyzes the oxygen …

In heme degradation catalyzed by the reconstituted heme oxygenase system, 8 to 9 mol of
dioxygen and 11 to 12 mol of NADPH were consumed per mol of hemin lost, and about half …

Covering: up to 2006 Heme oxygenase (HO) catalyzes O2-dependent regiospecific
conversion of heme to biliverdin, CO and free Fe (II). The heme group is tightly sandwiched …

Heme oxygenase (HO) is an enzyme that catalyzes the regiospecific conversion of heme to
biliverdin IXα, CO, and free iron. In mammals, HO has a variety of physiological functions …