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 …

The crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate
(biliverdin (Fe)-HO-1), the immediate precursor of the final product, biliverdin, has been …

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 …

Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to biliverdin by utilizing O2
and NADPH. HO (apoHO) was crystallized as twinned P 32 with three molecules per …

Heme oxygenase (HO) catalyzes the degradation of heme to biliverdin. The crystal structure
of human HO-1 in complex with heme reveals a novel helical structure with conserved …

Heme oxygenase (HO) catalyzes heme degradation by utilizing O2 and reducing
equivalents to produce biliverdin IXα, iron, and CO. To avoid product inhibition, the heme …

The crystal structure of heme oxygenase-1 suggests that Asp-140 may participate in a
hydrogen bonding network involving ligands coordinated to the heme iron atom. To examine …

The heme oxygenase (HO) system degrades heme to biliverdin and CO and releases
chelated iron. In the primary sequence of the constitutive form, HO-2, there are three …

Heme oxygenase oxidatively degrades heme to biliverdin resulting in the release of iron and
CO through a process in which the heme participates both as a cofactor and substrate. One …

A truncated, soluble rat heme oxygenase-1 lacking its C-terminal, membrane-anchoring
segment, and its His25→ Ala and His132→ Ala mutants have been prepared by site …