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Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1] Heme is biosynthesized in both the bone marrow and ...
Heme is a major source of dietary iron in humans and other mammals, and its synthesis in the body is well understood, but heme pathways are not as well understood. It is likely that heme is tightly regulated for two reasons: the toxic nature of iron in cells, and the lack of a regulated excretory system for excess iron.
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Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. [1] It is a cofactor at the active site of sulfite reductase , which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide , which can be incorporated into the ...
Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood.
Heme oxygenase 1 (HMOX1, commonly HO-1) is a member of the heat shock protein (HSP) family identified as HSP32.HO-1 is a 32kDa enzyme which contains 288 amino acid residues encoded by the HMOX1 gene.
Heme B is an essential cofactor in many proteins and enzymes. In particular, heme b plays a key role as the oxygen carrier in hemoglobin in red blood cells and myoglobin in muscle cells. Furthermore, heme B is found in cytochrome b , a key component in Q-cytochrome c oxidoreductase (complex III) in oxidative phosphorylation .
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