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Other oxygen-binding proteins

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Myoglobin Found in the muscle tissue of many vertebrates, including humans, it gives muscle tissue a distinct red or dark gray color. It is very similar to hemoglobin in structure and sequence, but is not a tetramer; instead, it is a monomer that lacks cooperative binding. It is used to store oxygen rather than transport it. Hemocyanin The second most common oxygen-transporting protein found in nature, it is found in the blood of many arthropods and molluscs. Uses copper prosthetic groups instead of iron heme groups and is blue in color when oxygenated. Hemerythrin Some marine invertebrates and a few species of annelid use this iron-containing non-heme protein to carry oxygen in their blood. Appears pink/violet when oxygenated, clear when not. Chlorocruorin Found in many annelids, it is very similar to erythrocruorin, but the heme group is significantly different in structure. Appears green when deoxygenated and red when oxygenated. Vanabins Also known as vanadium chromagens , the...
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In history, art and music

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Historically, an association between the color of blood and rust occurs in the association of the planet Mars, with the Roman god of war, since the planet is an orange-red, which reminded the ancients of blood. Although the color of the planet is due to iron compounds in combination with oxygen in the Martian soil, it is a common misconception that the iron in hemoglobin and its oxides gives blood its red color. The color is actually due to the porphyrin moiety of hemoglobin to which the iron is bound, not the iron itself, although the ligation and redox state of the iron can influence the pi to pi* or n to pi* electronic transitions of the porphyrin and hence its optical characteristics. Artist Julian Voss-Andreae created a sculpture called Heart of Steel (Hemoglobin) in 2005, based on the protein's backbone. The sculpture was made from glass and weathering steel. The intentional rusting of the initially shiny work of art mirrors hemoglobin's fundamental chemical reaction of ...
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Types in humans

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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 in 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 (ζ 2 ε 2 ) Gower 2 (α 2 ε 2 ) ( PDB: 1A9W ​) Hemoglobin Portland I (ζ 2 γ 2 ) Hemoglobin Portland II (ζ 2 β 2 ). In the fetus: Hemoglobin F (α 2 γ 2 ) ( PDB: 1FDH ​). After birth: Hemoglobin A (adult hemoglobin) (α 2 β 2 ) ( PDB: 1BZ0 ​) – The most common with a normal amount over 95% Hemoglobin A 2 (α 2 δ 2 ) – 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) (α 2 γ 2 ) – In adults Hemoglobin F is restricted to a limited population of red cells called F-cells. Howev...
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