Heme oxygenase (HO) is responsible for the physiological breakdown of heme into
equimolar amounts of biliverdin, carbon monoxide, and iron. Three isoforms (HO‐1, HO‐2 …

In biological systems oxidation of heme is carried out by two isozymes of the microsomal
heme oxygenase, HO‐1 and HO‐2. HO‐1 is the commonly known heme oxygenase, the …

Heme oxygenase-1 (HO-1) catalyzes the degradation of heme and forms antioxidant bile
pigments as well as the signaling molecule carbon monoxide. HO-1 is inducible in response …

Hemeoxygenase (HO) system is responsible for cellular heme degradation to biliverdin,
iron, and carbon monoxide. Two isoforms have been reported to date. Homologous HO‐1 …

Heme oxygenase-1 (HO-1), a ubiquitous inducible stress-response protein, serves a major
metabolic function in heme turnover. HO activity cleaves heme to form biliverdin-IXα, carbon …

Heme oxygenase (HO) catalyzes the O 2-and NADPH-dependent conversion of heme to
biliverdin, CO, and iron. The two forms of HO (HO-1 and HO-2) share similar physical …

Abstract Heme oxygenase isozymes, HO-1, HO-2 and HO-3, are HSP32 protein cognates,
with a known function of catalyzing the isomer specific oxidation of the heme molecule …

Significance: Heme oxygenase-1 (HO-1) is a ubiquitous 32-kDa protein expressed in many
tissues and highly inducible. They catalyze the degradation of the heme group and the …

HO-1 (haem oxygenase-1) is a ubiquitously expressed inducible enzyme degrading haem
to CO, biliverdin and Fe2+. Its activation reduces oxidative stress in cells and inhibits …

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 …