Heme oxygenases (HO) catabolize free heme, that is, iron (Fe) protoporphyrin (IX), into
equimolar amounts of Fe2+, carbon monoxide (CO), and biliverdin. The stress-responsive …

Heme oxygenase (HO)-1 catalyzes the oxidative cleavage of heme to yield equimolar
amounts of biliverdin, iron, and carbon monoxide. HO-1 is a stress response protein, the …

Abstract Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative
degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Biliverdin is …

Abstract Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide
(CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the …

Abstract Heme oxygenase (HO)-1, the inducible isoform of the heme-degrading enzyme HO,
plays a critical role in inflammation and iron homeostasis. Regulatory functions of HO-1 are …

Heme oxygenase (HO) catalyzes the oxidative cleavage of the α-mesocarbon of Fe-
protoporphyrin-IX yielding equimolar amounts of biliverdin-IXα, free divalent iron, and …

The HO-1 isoenzyme is an early stress response gene regulated by many forms of oxidative
stress. The HO-2 isoenzyme is predominantly a constitutive enzyme, which may serve to …

Heme oxygenase catalyzes the rate-limiting step in heme degradation in order to generate
biliverdin, carbon monoxide (CO), and iron. The inducible form of the enzyme, heme …

Heme oxygenase 1 (HO-1) inhibits apoptosis by regulating cellular prooxidant iron. We now
show that there is an additional mechanism by which HO-1 inhibits apoptosis, namely by …

Abstract Heme oxygenase-1 (HO-1), an inducible stress protein, confers cytoprotection
against oxidative stress in vitro and in vivo. In addition to its physiological role in heme …