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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | certain types of movement, and so are favored in the discipline of dressage. Some horseshoes have "caulkins", "caulks", or "calks": protrusions at the toe or heels of the shoe, or both, to provide additional traction.
When kept as a talisman, a horseshoe is said to bring good luck. A stylized variation of the horseshoe is used for a popular throwing game, horseshoes.
History
Since the early history of domestication of the horse, working animals were found to be exposed to many conditions that created br | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | eakage or excessive hoof wear. Ancient people recognized the need for the walls (and sometimes the sole) of domestic horses' hooves to have additional protection over and above any natural hardness. An early form of hoof protection was seen in ancient Asia, where horses' hooves were wrapped in rawhide, leather or other materials for both therapeutic purposes and protection from wear. From archaeological finds in Great Britain, the Romans appeared to have attempted to protect their horses' feet with a strap- | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | on, solid-bottomed "hipposandal" that has a slight resemblance to the modern hoof boot.
Historians differ on the origin of the horseshoe. Because iron was a valuable commodity, and any worn out items were generally reforged and reused, it is difficult to locate clear archaeological evidence. Although some credit the Druids, there is no hard evidence to support this claim. In 1897 four bronze horseshoes with what are apparently nail holes were found in an Etruscan tomb dated around 400 BC. The assertion by | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | some historians that the Romans invented the "mule shoes" sometime after 100 BC is supported by a reference by Catullus who died in 54 BC. However, these references to use of horseshoes and muleshoes in Rome may have been to the "hipposandal"—leather boots, reinforced by an iron plate, rather than to nailed horseshoes.
Existing references to the nailed shoe are relatively late, first known to have appeared around AD 900, but there may have been earlier uses given that some have been found in layers of dirt | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | . There are no extant references to nailed horseshoes prior to the reign of Byzantine Emperor Leo VI, and by 973 occasional references to them can be found. The earliest clear written record of iron horseshoes is a reference to "crescent figured irons and their nails" in AD 910. There is very little evidence of any sort that suggests the existence of nailed-on shoes prior to AD 500 or 600, though there is a find dated to the 5th century AD of a horseshoe, complete with nails, found in the tomb of the Franki | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | sh King Childeric I at Tournai, Belgium.
Around 1000 AD, cast bronze horseshoes with nail holes became common in Europe. A design with a scalloped outer rim and six nail holes was common. According to Gordon Ward the scalloped edges were created by double punching the nail holes causing the edges to bulge. The 13th and 14th centuries brought the widespread manufacturing of iron horseshoes. By the time of the Crusades (1096–1270), horseshoes were widespread and frequently mentioned in various written sourc | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | es. In that period, due to the value of iron, horseshoes were even accepted in lieu of coin to pay taxes.
By the 13th century, shoes were forged in large quantities and could be bought ready-made. Hot shoeing, the process of shaping a heated horseshoe immediately before placing it on the horse, became common in the 16th century. From the need for horseshoes, the craft of blacksmithing became "one of the great staple crafts of medieval and modern times and contributed to the development of metallurgy." A tr | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | eatise titled "No Foot, No Horse" was published in England in 1751.
In 1835, the first U.S. patent for a horseshoe manufacturing machine capable of making up to 60 horseshoes per hour was issued to Henry Burden. In mid-19th-century Canada, marsh horseshoes kept horses from sinking into the soft intertidal mud during dike-building. In a common design, a metal horseshoe holds a flat wooden shoe in place.
China
In China, iron horseshoes became common during the Yuan dynasty (1271–1368), prior to which rattan | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | and leather shoes were used to preserve animal hooves. Evidence of the preservation of horse hooves in China dates to the Warring States period (476–221 BC), during which Zhuangzi recommended shaving horse hooves to keep them in good shape. The Discourses on Salt and Iron in 81 BC mentions using leather shoes, but it's not clear if they were used for protecting horse hooves or to aid in mounting the horse. Remnants of iron horseshoes have been found in what is now northeast China, but the tombs date to the | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | Goguryeo period in 414 AD. A mural in the Mogao Caves dated to 584 AD depicts a man caring for a horse's hoof, which some speculate might be depicting horseshoe nailing, but the mural is too eroded to tell clearly.
The earliest reference to iron horseshoes in China dates to 938 AD during the Five Dynasties and Ten Kingdoms period. A monk named Gao Juhui sent to the Western Regions writes that the people in Ganzhou (now Zhangye) taught him how to make "horse hoof muse", which had four holes in it that conn | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | ected to four holes in the horse's hoof, and were thus put together. They also recommended using yak skin shoes for camel hooves. Iron horseshoes however did not become common for another three centuries. Zhao Rukuo writes in Zhu Fan Zhi, finished in 1225, that the horses of the Arabs and Persians used metal for horse shoes, implying that horses in China did not. After the establishment of the Yuan dynasty in 1271 AD, iron horseshoes became more common in northern China. When Thomas Blakiston travelled up t | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | he Yangtze, he noted that in Sichuan "cattle wore straw shoes to prevent their slipping on the wet ground" while in northern China, "horses and cattle are shod with iron shoes and nails." The majority of Chinese horseshoe discoveries have been in Jilin, Heilongjiang, Liaoning, Sichuan, and Tibet.
Reasons for use
Environmental changes linked to domestication
Many changes brought about by the domestication of the horse have led to a need for shoes for numerous reasons, mostly linked to management that resu | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | lts in horses' hooves hardening less and being more vulnerable to injury. In the wild, a horse may travel up to per day to obtain adequate forage. While horses in the wild cover large areas of terrain, they usually do so at relatively slow speeds, unless being chased by a predator. They also tend to live in arid steppe climates. The consequence of slow but nonstop travel in a dry climate is that horses' feet are naturally worn to a small, smooth, even and hard state. The continual stimulation of the sole o | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | f the foot keeps it thick and hard. However, in domestication, the ways horses are used differ from what they would encounter in their natural environment. Domesticated horses are brought to colder and wetter areas than their ancestral habitat. These softer and heavier soils soften the hooves and make them prone to splitting, making hoof protection necessary. Consequently, it was in northern Europe that the nailed horseshoe arose in its modern form.
Physical stresses requiring horseshoes
Abnormal stress: H | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | orses' hooves can become quite worn out when subjected to the added weight and stress of a rider, pack load, cart, or wagon.
Corrective shoeing: The shape, weight, and thickness of a horseshoe can significantly affect the horse's gait. Farriers may forge custom shoes to help horses with bone or musculature problems in their legs, or fit commercially available remedial shoes.
Traction: Traction devices such as borium for ice, horse shoe studs for muddy or slick conditions, calks, carbide-tipped road nails a | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | nd rims are useful for performance horses such as eventers, show jumpers, polo ponies, and other horses that perform at high speeds, over changing terrain, or in less-than-ideal footing.
Gait manipulation: Some breeds such as the Saddlebred, Tennessee Walking Horse, and other gaited horses are judged on their high-stepping movement. Special shoeing can help enhance their natural movement.
Racing horses with weakness in their foot or leg require specialized horseshoes.
Horseshoeing theories and debates
Do | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | mestic horses do not always require shoes. When possible, a "barefoot" hoof, at least for part of every year, is a healthy option for most horses. However, horseshoes have their place and can help prevent excess or abnormal hoof wear and injury to the foot. Many horses go without shoes year-round, some using temporary protection such as hoof boots for short-term use.
Process of shoeing
Shoeing, when performed correctly, causes no pain to the animal. Farriers trim the insensitive part of the hoof, which is | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | the same area into which they drive the nails. This is analogous to a manicure on a human fingernail, only on a much larger scale.
Before beginning to shoe, the farrier removes the old shoe using pincers (shoe pullers) and trims the hoof wall to the desired length with nippers, a sharp pliers-like tool, and the sole and frog of the hoof with a hoof knife. Shoes do not allow the hoof to wear down as it naturally would in the wild, and it can then become too long. The coffin bone inside the hoof should line | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | up straight with both bones in the pastern. If the excess hoof is not trimmed, the bones will become misaligned, which would place stress on the legs of the animal.
Shoes are then measured to the foot and bent to the correct shape using a hammer, anvil, forge, and other modifications, such as taps for shoe studs, are added. Farriers may either cold shoe, in which they bend the metal shoe without heating it, or hot shoe, in which they place the metal in a forge before bending it. Hot shoeing can be more t | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | ime-consuming, and requires the farrier to have access to a forge; however, it usually provides a better fit, as the mark made on the hoof from the hot shoe can show how even it lies. It also allows the farrier to make more modifications to the shoe, such as drawing toe- and quarter-clips. The farrier must take care not to hold the hot shoe against the hoof too long, as the heat can damage the hoof.
Hot shoes are placed in water to cool them off. The farrier then nails the shoes on, by driving the nails in | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | to the hoof wall at the white line of the hoof. The nails are shaped in such a way that they bend outward as they are driven in, avoiding the sensitive inner part of the foot, so they emerge on the sides of the hoof. When the nail has been completely driven, the farrier cuts off the sharp points and uses a clincher (a form of tongs made especially for this purpose) or a clinching block with hammer to bend the rest of the nail so it is almost flush with the hoof wall. This prevents the nail from getting caug | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | ht on anything, and also helps to hold the nail, and therefore the shoe, in place.
The farrier then uses a rasp (large file), to smooth the edge where it meets the shoe and eliminate any sharp edges left from cutting off the nails.
In culture
Superstition
Horseshoes have long been considered lucky. They were originally made of iron, a material that was believed to ward off evil spirits, and traditionally were held in place with seven nails, seven being the luckiest number. The superstition acquired a fu | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | rther Christian twist due to a legend surrounding the 10th-century saint Dunstan, who worked as a blacksmith before becoming Archbishop of Canterbury. The legend recounts that, one day, the Devil walked into Dunstan's shop and asked him to shoe his horse. Dunstan pretended not to recognize him, and agreed to the request; but rather than nailing the shoe to the horse's hoof, he nailed it to the Devil's own foot, causing him great pain. Dunstan eventually agreed to remove the shoe, but only after extracting a | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | promise that the Devil would never enter a household with a horseshoe nailed to the door.
Opinion is divided as to which way up the horseshoe ought to be nailed. Some say the ends should point up, so that the horseshoe catches the luck, and that the ends pointing down allow the good luck to be lost; others say they should point down, so that the luck is poured upon those entering the home.
Superstitious sailors believe that nailing a horseshoe to the mast will help their vessel avoid storms.
Heraldry
In | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | heraldry, horseshoes most often occur as canting charges, such as in the arms of families with names like Farrier, Marshall and Smith. A horseshoe (together with two hammers) also appears in the arms of Hammersmith and Fulham, a borough in London.
The flag of Rutland, England's smallest historic county, consists of a golden horseshoe laid over a field scattered with acorns. This references an ancient tradition in which every noble visiting Oakham, Rutland's county town, presents a horseshoe to the Lord of | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | the Manor, which is then nailed to the wall of Oakham Castle. Over the centuries, the Castle has amassed a vast collection of horseshoes, the oldest of which date from the 15th century.
The arms of Espoo, Finland are Azure, a crowned horseshoe Or.
Monuments and structures
The massive golden horseshoe structure is erected over the shopping mall of the Tuuri village in Alavus, a town of Finland. It is one of the most famous monuments in the locality; however, it stands at number three in Reuters' list of w | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | orld's ugliest buildings and monuments.
Sport
The sport of horseshoes involves a horseshoe being thrown as close as possible to a rod in order to score points. As far as it is known, the sport is as old as horseshoes themselves. While traditional horseshoes can still be used, most organized versions of the game use specialized sport horseshoes, which do not fit on horses' hooves.
See also
Farrier
Horse care
Horse hoof
Laminitis
Natural hoof care
References
External links
Historical development of the | [
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13480 | https://en.wikipedia.org/wiki/Horseshoe | Horseshoe | horseshoe 1891 Scientific American article from Project Gutenberg
The True Legend of St. Dunstan and the Devil by Edward G. Flight, illustrated by George Cruikshank, published in 1871, and available from Project Gutenberg
Mair and Dicken collections of historical horseshoes in the Museum of English Rural Life
Equine hoof
Heraldic charges
Lucky symbols
Farriery
Objects believed to protect from evil
Talismans | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | Hemoglobin, (haemoglobin BrE) (from the Greek word αἷμα, haîma 'blood' + Latin globus 'ball, sphere' + -in) (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues). There it releases the oxygen to permit aerobic respira | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | tion to provide energy to power the functions of the organism in the process called metabolism. A healthy individual has 12 to 20 grams of hemoglobin in every 100 mL of blood.
In mammals, the protein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34 mL O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglob | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | in molecule can bind (carry) up to four oxygen molecules.
Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20–25% of the total) as carbaminohemoglobin, in which CO2 is bound to the heme protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen.
Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells th | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | at contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, lungs, retinal pigment epithelium, hepatocytes, mesangial cells in the kidney, endometrial cells, cervical cells and vaginal epithelial cells. In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism. Excessive glucose in one's blood can attach to hemoglobin and raise the level of hemoglobin A1c.
Hemoglobin and hemoglobin-like molecules | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge oxygen away from anaerobic systems, such as the nitrogen-fixing nodules of leguminous plants, lest the oxygen poison (deactivate) the system.
Hemoglobinemia is a medical condition in which there | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | is an excess of hemoglobin in the blood plasma. This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia.
Research history
In 1825, Johann Friedrich Engelhart discovered that the ratio of iron to protein is identical in the hemoglobins of several species. From the known atomic mass of iron he calculated the molecular mass of hemoglobin to n × 16000 (n = number of iron atoms per hemoglobin, now known to be 4), the first determination of a protein's | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | molecular mass. This "hasty conclusion" drew a lot of ridicule at the time from scientists who could not believe that any molecule could be that big. Gilbert Smithson Adair confirmed Engelhart's results in 1925 by measuring the osmotic pressure of hemoglobin solutions.
Although blood had been known to carry oxygen since at least 1794, the oxygen-carrying property of hemoglobin was described by Hünefeld in 1840. In 1851, German physiologist Otto Funke published a series of articles in which he described gr | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | owing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution. Hemoglobin's reversible oxygenation was described a few years later by Felix Hoppe-Seyler.
In 1959, Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography. This work resulted in his sharing with John Kendrew the 1962 Nobel Prize in Chemistry for their studies of the structures of | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | globular proteins.
The role of hemoglobin in the blood was elucidated by French physiologist Claude Bernard.
The name hemoglobin is derived from the words heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group. Each heme group contains one iron atom, that can bind one oxygen molecule through ion-induced dipole forces. The most common type of hemoglobin in mammals contains four such subunits.
Genetics
Hemoglobin consists of protein subunits | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | (the globin molecules), and these proteins, in turn, are folded chains of a large number of different amino acids called polypeptides. The amino acid sequence of any polypeptide created by a cell is in turn determined by the stretches of DNA called genes. In all proteins, it is the amino acid sequence that determines the protein's chemical properties and function.
There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present in adult) is coded for by the genes, HBA1, | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | HBA2, and HBB. The hemoglobin subunit alpha 1 and alpha 2 are coded by the genes HBA1 and HBA2, respectively, which are both on chromosome 16 and are close to each other. The hemoglobin subunit beta is coded by HBB gene which is on chromosome 11 . The amino acid sequences of the globin proteins in hemoglobins usually differ between species. These differences grow with evolutionary distance between species. For example, the most common hemoglobin sequences in humans, bonobos and chimpanzees are completely i | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | dentical, without even a single amino acid difference in either the alpha or the beta globin protein chains. Whereas the human and gorilla hemoglobin differ in one amino acid in both alpha and beta chains, these differences grow larger between less closely related species.
Even within species, variants of hemoglobin exist, although one sequence is usually "most common" in each species. Mutations in the genes for the hemoglobin protein in a species result in hemoglobin variants. Many of these mutant forms o | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | f hemoglobin cause no disease. Some of these mutant forms of hemoglobin, however, cause a group of hereditary diseases termed the hemoglobinopathies. The best known hemoglobinopathy is sickle-cell disease, which was the first human disease whose mechanism was understood at the molecular level. A (mostly) separate set of diseases called thalassemias involves underproduction of normal and sometimes abnormal hemoglobins, through problems and mutations in globin gene regulation. All these diseases produce anemi | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | a.
Variations in hemoglobin amino acid sequences, as with other proteins, may be adaptive. For example, hemoglobin has been found to adapt in different ways to high altitudes. Organisms living at high elevations experience lower partial pressures of oxygen compared to those at sea level. This presents a challenge to the organisms that inhabit such environments because hemoglobin, which normally binds oxygen at high partial pressures of oxygen, must be able to bind oxygen when it is present at a lower press | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ure. Different organisms have adapted to such a challenge. For example, recent studies have suggested genetic variants in deer mice that help explain how deer mice that live in the mountains are able to survive in the thin air that accompanies high altitudes. A researcher from the University of Nebraska-Lincoln found mutations in four different genes that can account for differences between deer mice that live in lowland prairies versus the mountains. After examining wild mice captured from both highlands a | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | nd lowlands, it was found that: the genes of the two breeds are "virtually identical—except for those that govern the oxygen-carrying capacity of their hemoglobin". "The genetic difference enables highland mice to make more efficient use of their oxygen", since less is available at higher altitudes, such as those in the mountains. Mammoth hemoglobin featured mutations that allowed for oxygen delivery at lower temperatures, thus enabling mammoths to migrate to higher latitudes during the Pleistocene. This wa | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | s also found in hummingbirds that inhabit the Andes. Hummingbirds already expend a lot of energy and thus have high oxygen demands and yet Andean hummingbirds have been found to thrive in high altitudes. Non-synonymous mutations in the hemoglobin gene of multiple species living at high elevations (Oreotrochilus, A. castelnaudii, C. violifer, P. gigas, and A. viridicuada) have caused the protein to have less of an affinity for inositol hexaphosphate (IHP), a molecule found in birds that has a similar role as | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | 2,3-BPG in humans; this results in the ability to bind oxygen in lower partial pressures.
Birds' unique circulatory lungs also promote efficient use of oxygen at low partial pressures of O2. These two adaptations reinforce each other and account for birds' remarkable high-altitude performance.
Hemoglobin adaptation extends to humans, as well. There is a higher offspring survival rate among Tibetan women with high oxygen saturation genotypes residing at 4,000 m. Natural selection seems to be the main forc | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | e working on this gene because the mortality rate of offspring is significantly lower for women with higher hemoglobin-oxygen affinity when compared to the mortality rate of offspring from women with low hemoglobin-oxygen affinity. While the exact genotype and mechanism by which this occurs is not yet clear, selection is acting on these women's ability to bind oxygen in low partial pressures, which overall allows them to better sustain crucial metabolic processes.
Synthesis
Hemoglobin (Hb) is synthesized i | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | n a complex series of steps. The heme part is synthesized in a series of steps in the mitochondria and the cytosol of immature red blood cells, while the globin protein parts are synthesized by ribosomes in the cytosol. Production of Hb continues in the cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow. At this point, the nucleus is lost in mammalian red blood cells, but not in birds and many other species. Even after the loss of the nucleus in mammals, re | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | sidual ribosomal RNA allows further synthesis of Hb until the reticulocyte loses its RNA soon after entering the vasculature (this hemoglobin-synthetic RNA in fact gives the reticulocyte its reticulated appearance and name).
Structure of heme
Hemoglobin has a quaternary structure characteristic of many multi-subunit globular proteins. Most of the amino acids in hemoglobin form alpha helices, and these helices are connected by short non-helical segments. Hydrogen bonds stabilize the helical sections insid | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | e this protein, causing attractions within the molecule, which then causes each polypeptide chain to fold into a specific shape. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.
In most vertebrates, the hemoglobin molecule is an assembly of four globular protein subunits. Each subunit is composed of a protein chain tightly associated with a non-protein prosthetic heme group. Each protein chain arranges into a set of alpha-helix structural segments connect | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ed together in a globin fold arrangement. Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin. This folding pattern contains a pocket that strongly binds the heme group.
A heme group consists of an iron (Fe) ion held in a heterocyclic ring, known as a porphyrin. This porphyrin ring consists of four pyrrole molecules cyclically linked together (by methine bridges) with the iron ion bound in the center. The iron ion, which is the site o | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | f oxygen binding, coordinates with the four nitrogen atoms in the center of the ring, which all lie in one plane. The heme is bound strongly (covalently) to the globular protein via the N atoms of the imidazole ring of F8 histidine residue (also known as the proximal histidine) below the porphyrin ring. A sixth position can reversibly bind oxygen by a coordinate covalent bond, completing the octahedral group of six ligands. This reversible bonding with oxygen is why hemoglobin is so useful for transporting | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | oxygen around the body. Oxygen binds in an "end-on bent" geometry where one oxygen atom binds to Fe and the other protrudes at an angle. When oxygen is not bound, a very weakly bonded water molecule fills the site, forming a distorted octahedron.
Even though carbon dioxide is carried by hemoglobin, it does not compete with oxygen for the iron-binding positions but is bound to the amine groups of the protein chains attached to the heme groups.
The iron ion may be either in the ferrous Fe2+ or in the ferric | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | Fe3+ state, but ferrihemoglobin (methemoglobin) (Fe3+) cannot bind oxygen. In binding, oxygen temporarily and reversibly oxidizes (Fe2+) to (Fe3+) while oxygen temporarily turns into the superoxide ion, thus iron must exist in the +2 oxidation state to bind oxygen. If superoxide ion associated to Fe3+ is protonated, the hemoglobin iron will remain oxidized and incapable of binding oxygen. In such cases, the enzyme methemoglobin reductase will be able to eventually reactivate methemoglobin by reducing the i | [
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] |
13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ron center.
In adult humans, the most common hemoglobin type is a tetramer (which contains four subunit proteins) called hemoglobin A, consisting of two α and two β subunits non-covalently bound, each made of 141 and 146 amino acid residues, respectively. This is denoted as α2β2. The subunits are structurally similar and about the same size. Each subunit has a molecular weight of about 16,000 daltons, for a total molecular weight of the tetramer of about 64,000 daltons (64,458 g/mol). Thus, 1 g/dL = 0.1551 | [
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] |
13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | mmol/L. Hemoglobin A is the most intensively studied of the hemoglobin molecules.
In human infants, the hemoglobin molecule is made up of 2 α chains and 2 γ chains. The γ chains are gradually replaced by β chains as the infant grows.
The four polypeptide chains are bound to each other by salt bridges, hydrogen bonds, and the hydrophobic effect.
Oxygen saturation
In general, hemoglobin can be saturated with oxygen molecules (oxyhemoglobin), or desaturated with oxygen molecules (deoxyhemoglobin).
Oxyhemo | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | globin
Oxyhemoglobin is formed during physiological respiration when oxygen binds to the heme component of the protein hemoglobin in red blood cells. This process occurs in the pulmonary capillaries adjacent to the alveoli of the lungs. The oxygen then travels through the blood stream to be dropped off at cells where it is utilized as a terminal electron acceptor in the production of ATP by the process of oxidative phosphorylation. It does not, however, help to counteract a decrease in blood pH. Ventilation | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | , or breathing, may reverse this condition by removal of carbon dioxide, thus causing a shift up in pH.
Hemoglobin exists in two forms, a taut (tense) form (T) and a relaxed form (R). Various factors such as low pH, high CO2 and high 2,3 BPG at the level of the tissues favor the taut form, which has low oxygen affinity and releases oxygen in the tissues. Conversely, a high pH, low CO2, or low 2,3 BPG favors the relaxed form, which can better bind oxygen. The partial pressure of the system also affects O2 a | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ffinity where, at high partial pressures of oxygen (such as those present in the alveoli), the relaxed (high affinity, R) state is favoured. Inversely, at low partial pressures (such as those present in respiring tissues), the (low affinity, T) tense state is favoured. Additionally, the binding of oxygen to the iron(II) heme pulls the iron into the plane of the porphyrin ring, causing a slight conformational shift. The shift encourages oxygen to bind to the three remaining heme units within hemoglobin (thus | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | , oxygen binding is cooperative).
Deoxygenated hemoglobin
Deoxygenated hemoglobin (deoxyhemoglobin) is the form of hemoglobin without the bound oxygen. The absorption spectra of oxyhemoglobin and deoxyhemoglobin differ. The oxyhemoglobin has significantly lower absorption of the 660 nm wavelength than deoxyhemoglobin, while at 940 nm its absorption is slightly higher. This difference is used for the measurement of the amount of oxygen in a patient's blood by an instrument called a pulse oximeter. This diff | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | erence also accounts for the presentation of cyanosis, the blue to purplish color that tissues develop during hypoxia.
Deoxygenated hemoglobin is paramagnetic; it is weakly attracted to magnetic fields. In contrast, oxygenated hemoglobin exhibits diamagnetism, a weak repulsion from a magnetic field.
Evolution of vertebrate hemoglobin
Scientists agree that the event that separated myoglobin from hemoglobin occurred after lampreys diverged from jawed vertebrates. This separation of myoglobin and hemoglobin | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | allowed for the different functions of the two molecules to arise and develop: myoglobin has more to do with oxygen storage while hemoglobin is tasked with oxygen transport. The α- and β-like globin genes encode the individual subunits of the protein. The predecessors of these genes arose through another duplication event also after the gnathosome common ancestor derived from jawless fish, approximately 450–500 million years ago. Ancestral reconstruction studies suggest that the preduplication ancestor of | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | the α and β genes was a dimer made up of identical globin subunits, which then evolved to assemble into a tetrameric architecture after the duplication. The development of α and β genes created the potential for hemoglobin to be composed of multiple distinct subunits, a physical composition central to hemoglobin's ability to transport oxygen. Having multiple subunits contributes to hemoglobin's ability to bind oxygen cooperatively as well as be regulated allosterically. Subsequently, the α gene also underwe | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | nt a duplication event to form the HBA1 and HBA2 genes. These further duplications and divergences have created a diverse range of α- and β-like globin genes that are regulated so that certain forms occur at different stages of development.
Most ice fish of the family Channichthyidae have lost their hemoglobin genes as an adaptation to cold water.
Iron's oxidation state in oxyhemoglobin
Assigning oxygenated hemoglobin's oxidation state is difficult because oxyhemoglobin (Hb-O2), by experimental measuremen | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | t, is diamagnetic (no net unpaired electrons), yet the lowest-energy (ground-state) electron configurations in both oxygen and iron are paramagnetic (suggesting at least one unpaired electron in the complex). The lowest-energy form of oxygen, and the lowest energy forms of the relevant oxidation states of iron, are these:
Triplet oxygen, the lowest-energy molecular oxygen species, has two unpaired electrons in antibonding π* molecular orbitals.
Iron(II) tends to exist in a high-spin 3d6 configuration with | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | four unpaired electrons.
Iron(III) (3d5) has an odd number of electrons, and thus must have one or more unpaired electrons, in any energy state.
All of these structures are paramagnetic (have unpaired electrons), not diamagnetic. Thus, a non-intuitive (e.g., a higher-energy for at least one species) distribution of electrons in the combination of iron and oxygen must exist, in order to explain the observed diamagnetism and no unpaired electrons.
The two logical possibilities to produce diamagnetic (no n | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | et spin) Hb-O2 are:
Low-spin Fe2+ binds to singlet oxygen. Both low-spin iron and singlet oxygen are diamagnetic. However, the singlet form of oxygen is the higher-energy form of the molecule.
Low-spin Fe3+ binds to O2•− (the superoxide ion) and the two unpaired electrons couple antiferromagnetically, giving observed diamagnetic properties. Here, the iron has been oxidized (has lost one electron), and the oxygen has been reduced (has gained one electron).
Another possible model in which low-spin Fe4+ bi | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | nds to peroxide, O22−, can be ruled out by itself, because the iron is paramagnetic (although the peroxide ion is diamagnetic). Here, the iron has been oxidized by two electrons, and the oxygen reduced by two electrons.
Direct experimental data:
X-ray photoelectron spectroscopy suggests iron has an oxidation state of approximately 3.2.
Infrared vibrational frequencies of the O-O bond suggests a bond length fitting with superoxide (a bond order of about 1.6, with superoxide being 1.5).
X-ray Absorption N | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ear Edge Structures at the iron K-edge. The energy shift of 5 eV between deoxyhemoglobin and oxyhemoglobin, as for all the methemoglobin species, strongly suggests an actual local charge closer to Fe3+ than Fe2+.
Thus, the nearest formal oxidation state of iron in Hb-O2 is the +3 state, with oxygen in the −1 state (as superoxide .O2−). The diamagnetism in this configuration arises from the single unpaired electron on superoxide aligning antiferromagnetically with the single unpaired electron on iron (in a l | [
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] |
13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ow-spin d5 state), to give no net spin to the entire configuration, in accordance with diamagnetic oxyhemoglobin from experiment.
The second choice of the logical possibilities above for diamagnetic oxyhemoglobin being found correct by experiment, is not surprising: singlet oxygen (possibility #1) is an unrealistically high energy state. Model 3 leads to unfavorable separation of charge (and does not agree with the magnetic data), although it could make a minor contribution as a resonance form. Iron's shi | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ft to a higher oxidation state in Hb-O2 decreases the atom's size, and allows it into the plane of the porphyrin ring, pulling on the coordinated histidine residue and initiating the allosteric changes seen in the globulins.
Early postulates by bio-inorganic chemists claimed that possibility #1 (above) was correct and that iron should exist in oxidation state II. This conclusion seemed likely, since the iron oxidation state III as methemoglobin, when not accompanied by superoxide .O2− to "hold" the oxidati | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | on electron, was known to render hemoglobin incapable of binding normal triplet O2 as it occurs in the air. It was thus assumed that iron remained as Fe(II) when oxygen gas was bound in the lungs. The iron chemistry in this previous classical model was elegant, but the required presence of the diamagnetic, high-energy, singlet oxygen molecule was never explained. It was classically argued that the binding of an oxygen molecule placed high-spin iron(II) in an octahedral field of strong-field ligands; this ch | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ange in field would increase the crystal field splitting energy, causing iron's electrons to pair into the low-spin configuration, which would be diamagnetic in Fe(II). This forced low-spin pairing is indeed thought to happen in iron when oxygen binds, but is not enough to explain iron's change in size. Extraction of an additional electron from iron by oxygen is required to explain both iron's smaller size and observed increased oxidation state, and oxygen's weaker bond.
The assignment of a whole-number ox | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | idation state is a formalism, as the covalent bonds are not required to have perfect bond orders involving whole electron transfer. Thus, all three models for paramagnetic Hb-O2 may contribute to some small degree (by resonance) to the actual electronic configuration of Hb-O2. However, the model of iron in Hb-O2 being Fe(III) is more correct than the classical idea that it remains Fe(II).
Cooperativity
When oxygen binds to the iron complex, it causes the iron atom to move back toward the center of the pla | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ne of the porphyrin ring (see moving diagram). At the same time, the imidazole side-chain of the histidine residue interacting at the other pole of the iron is pulled toward the porphyrin ring. This interaction forces the plane of the ring sideways toward the outside of the tetramer, and also induces a strain in the protein helix containing the histidine as it moves nearer to the iron atom. This strain is transmitted to the remaining three monomers in the tetramer, where it induces a similar conformational | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | change in the other heme sites such that binding of oxygen to these sites becomes easier.
As oxygen binds to one monomer of hemoglobin, the tetramer's conformation shifts from the T (tense) state to the R (relaxed) state. This shift promotes the binding of oxygen to the remaining three monomer's heme groups, thus saturating the hemoglobin molecule with oxygen.
In the tetrameric form of normal adult hemoglobin, the binding of oxygen is, thus, a cooperative process. The binding affinity of hemoglobin for ox | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ygen is increased by the oxygen saturation of the molecule, with the first molecules of oxygen bound influencing the shape of the binding sites for the next ones, in a way favorable for binding. This positive cooperative binding is achieved through steric conformational changes of the hemoglobin protein complex as discussed above; i.e., when one subunit protein in hemoglobin becomes oxygenated, a conformational or structural change in the whole complex is initiated, causing the other subunits to gain an inc | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | reased affinity for oxygen. As a consequence, the oxygen binding curve of hemoglobin is sigmoidal, or S-shaped, as opposed to the normal hyperbolic curve associated with noncooperative binding.
The dynamic mechanism of the cooperativity in hemoglobin and its relation with low-frequency resonance has been discussed.
Binding for ligands other than oxygen
Besides the oxygen ligand, which binds to hemoglobin in a cooperative manner, hemoglobin ligands also include competitive inhibitors such as carbon monoxid | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | e (CO) and allosteric ligands such as carbon dioxide (CO2) and nitric oxide (NO). The carbon dioxide is bound to amino groups of the globin proteins to form carbaminohemoglobin; this mechanism is thought to account for about 10% of carbon dioxide transport in mammals. Nitric oxide can also be transported by hemoglobin; it is bound to specific thiol groups in the globin protein to form an S-nitrosothiol, which dissociates into free nitric oxide and thiol again, as the hemoglobin releases oxygen from its heme | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | site. This nitric oxide transport to peripheral tissues is hypothesized to assist oxygen transport in tissues, by releasing vasodilatory nitric oxide to tissues in which oxygen levels are low.
Competitive
The binding of oxygen is affected by molecules such as carbon monoxide (for example, from tobacco smoking, exhaust gas, and incomplete combustion in furnaces). CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen, meaning | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | that small amounts of CO dramatically reduce hemoglobin's ability to deliver oxygen to the target tissue. Since carbon monoxide is a colorless, odorless and tasteless gas, and poses a potentially fatal threat, carbon monoxide detectors have become commercially available to warn of dangerous levels in residences. When hemoglobin combines with CO, it forms a very bright red compound called carboxyhemoglobin, which may cause the skin of CO poisoning victims to appear pink in death, instead of white or blue. W | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | hen inspired air contains CO levels as low as 0.02%, headache and nausea occur; if the CO concentration is increased to 0.1%, unconsciousness will follow. In heavy smokers, up to 20% of the oxygen-active sites can be blocked by CO.
In similar fashion, hemoglobin also has competitive binding affinity for cyanide (CN−), sulfur monoxide (SO), and sulfide (S2−), including hydrogen sulfide (H2S). All of these bind to iron in heme without changing its oxidation state, but they nevertheless inhibit oxygen-binding | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | , causing grave toxicity.
The iron atom in the heme group must initially be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above). Initial oxidation to the ferric (Fe3+) state without oxygen converts hemoglobin into "hemiglobin" or methemoglobin, which cannot bind oxygen. Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. Nitric o | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | xide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells. The latter reaction is a remnant activity of the more ancient nitric oxide dioxygenase function of globins.
Allosteric
Carbon dioxide occupies a different binding site on the hemoglobin. At tissues, where carbon dioxide concentration is higher, carbon dioxide binds to allosteric site of hemoglobin, facilitating unloading of oxygen from hemoglobin and ultimately its removal from the body after the oxygen has b | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | een released to tissues undergoing metabolism. This increased affinity for carbon dioxide by the venous blood is known as the Bohr effect. Through the enzyme carbonic anhydrase, carbon dioxide reacts with water to give carbonic acid, which decomposes into bicarbonate and protons:
CO2 + H2O → H2CO3 → HCO3− + H+
Hence, blood with high carbon dioxide levels is also lower in pH (more acidic). Hemoglobin can bind protons and carbon dioxide, which causes a conformational change in the protein and facilitates th | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | e release of oxygen. Protons bind at various places on the protein, while carbon dioxide binds at the α-amino group. Carbon dioxide binds to hemoglobin and forms carbaminohemoglobin. This decrease in hemoglobin's affinity for oxygen by the binding of carbon dioxide and acid is known as the Bohr effect. The Bohr effect favors the T state rather than the R state. (shifts the O2-saturation curve to the right). Conversely, when the carbon dioxide levels in the blood decrease (i.e., in the lung capillaries), car | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | bon dioxide and protons are released from hemoglobin, increasing the oxygen affinity of the protein. A reduction in the total binding capacity of hemoglobin to oxygen (i.e. shifting the curve down, not just to the right) due to reduced pH is called the root effect. This is seen in bony fish.
It is necessary for hemoglobin to release the oxygen that it binds; if not, there is no point in binding it. The sigmoidal curve of hemoglobin makes it efficient in binding (taking up O2 in lungs), and efficient in unl | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | oading (unloading O2 in tissues).
In people acclimated to high altitudes, the concentration of 2,3-Bisphosphoglycerate (2,3-BPG) in the blood is increased, which allows these individuals to deliver a larger amount of oxygen to tissues under conditions of lower oxygen tension. This phenomenon, where molecule Y affects the binding of molecule X to a transport molecule Z, is called a heterotropic allosteric effect. Hemoglobin in organisms at high altitudes has also adapted such that it has less of an affinity | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | for 2,3-BPG and so the protein will be shifted more towards its R state. In its R state, hemoglobin will bind oxygen more readily, thus allowing organisms to perform the necessary metabolic processes when oxygen is present at low partial pressures.
Animals other than humans use different molecules to bind to hemoglobin and change its O2 affinity under unfavorable conditions. Fish use both ATP and GTP. These bind to a phosphate "pocket" on the fish hemoglobin molecule, which stabilizes the tense state and | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | therefore decreases oxygen affinity. GTP reduces hemoglobin oxygen affinity much more than ATP, which is thought to be due to an extra hydrogen bond formed that further stabilizes the tense state. Under hypoxic conditions, the concentration of both ATP and GTP is reduced in fish red blood cells to increase oxygen affinity.
A variant hemoglobin, called fetal hemoglobin (HbF, α2γ2), is found in the developing fetus, and binds oxygen with greater affinity than adult hemoglobin. This means that the oxygen bind | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ing curve for fetal hemoglobin is left-shifted (i.e., a higher percentage of hemoglobin has oxygen bound to it at lower oxygen tension), in comparison to that of adult hemoglobin. As a result, fetal blood in the placenta is able to take oxygen from maternal blood.
Hemoglobin also carries nitric oxide (NO) in the globin part of the molecule. This improves oxygen delivery in the periphery and contributes to the control of respiration. NO binds reversibly to a specific cysteine residue in globin; the binding | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | depends on the state (R or T) of the hemoglobin. The resulting S-nitrosylated hemoglobin influences various NO-related activities such as the control of vascular resistance, blood pressure and respiration. NO is not released in the cytoplasm of red blood cells but transported out of them by an anion exchanger called AE1.
Types in humans
Hemoglobin variants are a part of the normal embryonic and fetal development. They may also be pathologic mutant forms of hemoglobin in a population, caused by variations i | [
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] |
13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | n genetics. Some well-known hemoglobin variants, such as sickle-cell anemia, are responsible for diseases and are considered hemoglobinopathies. Other variants cause no detectable pathology, and are thus considered non-pathological variants.
In the embryo:
Gower 1 (ζ2ε2)
Gower 2 (α2ε2) ()
Hemoglobin Portland I (ζ2γ2)
Hemoglobin Portland II (ζ2β2).
In the fetus:
Hemoglobin F (α2γ2) ().
After birth:
Hemoglobin A (adult hemoglobin) (α2β2) () – The most common with a normal amount over 95%
Hemoglobin | [
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] |
13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | A2 (α2δ2) – δ chain synthesis begins late in the third trimester and, in adults, it has a normal range of 1.5–3.5%
Hemoglobin F (fetal hemoglobin) (α2γ2) – In adults Hemoglobin F is restricted to a limited population of red cells called F-cells. However, the level of Hb F can be elevated in persons with sickle-cell disease and beta-thalassemia.
Variant forms that cause disease:
Hemoglobin D-Punjab – (α2βD2) – A variant form of hemoglobin.
Hemoglobin H (β4) – A variant form of hemoglobin, formed by a tet | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ramer of β chains, which may be present in variants of α thalassemia.
Hemoglobin Barts (γ4) – A variant form of hemoglobin, formed by a tetramer of γ chains, which may be present in variants of α thalassemia.
Hemoglobin S (α2βS2) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which results in sickling of red blood cells.
Hemoglobin C (α2βC2) – Another variant due to a variation in the β-c | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | hain gene. This variant causes a mild chronic hemolytic anemia.
Hemoglobin E (α2βE2) – Another variant due to a variation in the β-chain gene. This variant causes a mild chronic hemolytic anemia.
Hemoglobin AS – A heterozygous form causing sickle cell trait with one adult gene and one sickle cell disease gene
Hemoglobin SC disease – A compound heterozygous form with one sickle gene and another encoding Hemoglobin C.
Hemoglobin Hopkins-2 – A variant form of hemoglobin that is sometimes viewed in combinat | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | ion with Hemoglobin S to produce sickle cell disease.
Degradation in vertebrate animals
When red blood cells reach the end of their life due to aging or defects, they are removed from the circulation by the phagocytic activity of macrophages in the spleen or the liver or hemolyze within the circulation. Free hemoglobin is then cleared from the circulation via the hemoglobin transporter CD163, which is exclusively expressed on monocytes or macrophages. Within these cells the hemoglobin molecule is broken up | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | , and the iron gets recycled. This process also produces one molecule of carbon monoxide for every molecule of heme degraded. 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. The other major final product of heme degradation is bilirubin. Increased levels of this chemical are detected in the blood if red blood cells are being destroyed more rapidly than usual. Improperly degrade | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | d hemoglobin protein or hemoglobin that has been released from the blood cells too rapidly can clog small blood vessels, especially the delicate blood filtering vessels of the kidneys, causing kidney damage. Iron is removed from heme and salvaged for later use, it is stored as hemosiderin or ferritin in tissues and transported in plasma by beta globulins as transferrins. When the porphyrin ring is broken up, the fragments are normally secreted as a yellow pigment called bilirubin, which is secreted into the | [
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13483 | https://en.wikipedia.org/wiki/Hemoglobin | Hemoglobin | intestines as bile. Intestines metabolise bilirubin into urobilinogen. Urobilinogen leaves the body in faeces, in a pigment called stercobilin. Globulin is metabolised into amino acids that are then released into circulation.
Diseases related to hemoglobin
Hemoglobin deficiency can be caused either by a decreased amount of hemoglobin molecules, as in anemia, or by decreased ability of each molecule to bind oxygen at the same partial pressure of oxygen. Hemoglobinopathies (genetic defects resulting in abn | [
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