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Heme. Binding of oxygen to a heme prosthetic group. 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.
A heme is an organic, ring-shaped molecule. Due to its special structure, a heme is capable of holding, or “hosting” an iron molecule. A heme is made from 4 pyrroles, which are small pentagon-shaped molecules made from 4 carbons and 1 nitrogen. Four pyrroles together form a tetrapyrrole.
Heme is a porphyrin ring complexed with ferrous iron and protoporphyrin IX. Heme is an essential prosthetic group in proteins that is necessary as a subcellular compartment to perform diverse biological functions like hemoglobin and myoglobin. [1]
Hemoglobin (Hb) is the most studied of the heme containing globulin proteins and yet is not fully understood. It was one of the first proteins to be studied by X-ray crystallography, and earned Max Perutz the Nobel Prize in Chemistry in 1962.
Hemoglobin, iron-containing protein in the blood of many animals that transports oxygen to the tissues. Hemoglobin forms an unstable reversible bond with oxygen. In the oxygenated state, it is called oxyhemoglobin and is bright red; in the reduced state, it is purplish blue.
This review offers a comprehensive analysis of the current literature on the health benefits and risks of heme as an essential nutrient. Heme constitutes 95% of the functional iron in the human body and accounts for two-thirds of iron intake for people in Western countries.
Heme (iron protoporphyrin IX) is an essential molecule for numerous living organisms. Not only does it serve as a prosthetic group in enzymes, it also acts as a signaling molecule that...
Heme is an iron-containing tetrapyrrole essential for diverse biological functions including gas transport and sensing, oxidative metabolism, and xenobiotic detoxification. Like iron, heme is essential yet toxic in excess. As such, both iron and heme homeostasis are tightly regulated.
Heme, an iron-containing tetrapyrrole in hemoproteins, including: hemoglobin, myoglobin, catalase, cytochrome c, and cytochrome P450, plays critical physiological roles in different organisms.
Hemoglobin synthesis requires the coordinated production of heme and globin. Heme is the prosthetic group that mediates reversible binding of oxygen by hemoglobin. Globin is the protein that surrounds and protects the heme molecule.