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In addition, heme degradation appears to be an evolutionarily-conserved response to oxidative stress. Briefly, when cells are exposed to free radicals , there is a rapid induction of the expression of the stress-responsive heme oxygenase-1 (HMOX1) isoenzyme that catabolizes heme (see below). [ 39 ]
Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous iron, and carbon monoxide. [ 1 ] There are many heme degrading enzymes in nature.
This process also produces one molecule of carbon monoxide for every molecule of heme degraded. [80] Heme degradation is the only natural source of carbon monoxide in the human body, and is responsible for the normal blood levels of carbon monoxide in people breathing normal air. [81] The other major final product of heme degradation is ...
Bilirubin (BR) (from the Latin for "red bile") is a red-orange compound that occurs in the normal catabolic pathway that breaks down heme in vertebrates.This catabolism is a necessary process in the body's clearance of waste products that arise from the destruction of aged or abnormal red blood cells. [3]
Biliverdin results from the breakdown of the heme moiety of hemoglobin in erythrocytes. Macrophages break down senescent erythrocytes and break the heme down into biliverdin along with hemosiderin, in which biliverdin normally rapidly reduces to free bilirubin. [1] [3] Biliverdin is seen briefly in some bruises as a green color.
Urobilin is generated from the degradation of heme, which is first degraded through biliverdin to bilirubin. Bilirubin is then excreted as bile, which is further degraded by microbes present in the large intestine to urobilinogen. The enzyme responsible for the degradation is bilirubin reductase, which was identified in 2024.
Indeed, research shows that only a small fraction of non-heme iron is absorbed by the body and more than 95% of functional iron in the human body is heme-iron. Maya Feller, ...
Protoporphyrin IX is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and chlorophylls. As a result, a number of organisms are able to synthesize this tetrapyrrole from basic precursors such as glycine and succinyl-CoA , or glutamic acid .