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Heme oxygenase (HO) catalyzes the degradation of heme. It is a membrane-bound enzyme that cleaves the heme ring at the α-methene bridge to produce bilverdin (which is metabolized further by bilirubin reductase to form bilirubin), iron and carbon monoxide.
Heme oxygenase (HO) catalyzes the degradation of heme. This membrane-bound enzyme cleaves the heme ring at the α-methene bridge to produce bilverdin (which is metabolized further by bilirubin reductase to form bilirubin), iron and the putative neurotransmitter, carbon monoxide.
There are three isoforms of heme oxygenase; the inducible HO-1, which is active at high concentrations of heme and at times of physiological stress, the constitutively active HO-2 and the non-catalytic HO-3, which is thought to function as an oxygen sensor. Heme oxygenase is localized to microsomes and the endoplasmic reticulum, and the enzyme is found at very high concentrations in splenocytes due to their function in the degradation of senescent erythrocytes.
Tocris offers the following scientific literature for Heme Oxygenase to showcase our products. We invite you to request* your copy today!
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