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 …

The oxidation of heme to biliverdin IXα by heme oxygenase involves regiospecific α-meso-
hydroxylation followed by extrusion of the α-meso-carbon as CO. In an earlier study …

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

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 …

R-meso-hydroxylation of the heme,(b) O2-dependent elimination of the R-meso-carbon as
CO with concomitant formation of verdoheme (1), and (c) NADPH-and O2-dependent …

A rat heme oxygenase (HO-1) gene without the sequence coding for the last 23 amino acids
has been constructed and expressed behind the pho A promoter in Escherichia coli. The …

Heme IX (iron (II) protoporphyrin IX)(1) is an important metabolite involved in the regulation
of globin synthesis, 1 in the expression of human transferrin re-ceptors, 2 in the regulation of …

Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to involve α-
meso-hydroxylation and elimination of the meso-carbon as CO, a reaction supported by both …

Heme oxygenase regiospecifically oxidizes heme at the α-meso position to give biliverdin
IXα, CO, and iron. The heme orientation within the active site, which is thought to determine …