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 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 …

Heme oxygenase converts heme to biliverdin, iron, and CO in a reaction with two
established intermediates, α-meso-hydroxyheme and verdoheme. Transient kinetic studies …

The oxidation of heme by heme oxygenase (HO-1) results in highly regiospecific extrusion of
the α-meso-carbon as CO and the formation of biliverdin IXα. The first step in the accepted …

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 (HO) catalyzes the degradation of heme to biliverdinIXR (R-biliverdin),
CO, and free iron by three sequential reactions which require O2, NADPH, and cytochrome …

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 …

Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of
heme metabolism utilizing O2 and NADPH. We determined the crystal structures of rat heme …

Heme oxygenase oxidatively cleaves heme to biliverdin, leading to the release of iron and
CO through a process in which the heme participates both as a cofactor and as a substrate …