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The human body needs iron for oxygen transport. Oxygen (O 2) is required for the functioning and survival of nearly all cell types. Oxygen is transported from the lungs to the rest of the body bound to the heme group of hemoglobin in red blood cells. In muscles cells, iron binds oxygen to myoglobin, which regulates its release.
Iron-containing proteins participate in transport, storage and use of oxygen. [1] Iron proteins are involved in electron transfer . [ 5 ] The ubiquity of Iron in life has led to the Iron–sulfur world hypothesis that iron was a central component of the environment of early life.
The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group.
The oxide mineral class includes those minerals in which the oxide anion (O 2−) is bonded to one or more metal alloys. The hydroxide -bearing minerals are typically included in the oxide class. Minerals with complex anion groups such as the silicates , sulfates , carbonates and phosphates are classed separately.
In vertebrates, an essential member of the porphyrin group is heme, which is a component of hemoproteins, whose functions include carrying oxygen in the bloodstream. In plants, an essential porphyrin derivative is chlorophyll, which is involved in light harvesting and electron transfer in photosynthesis.
Copper proteins have diverse roles in biological electron transport and oxygen transportation, processes that exploit the easy interconversion of Cu(I) and Cu(II). [2] Copper is essential in the aerobic respiration of all eukaryotes. In mitochondria, it is found in cytochrome c oxidase, which is the last protein in oxidative phosphorylation.
The oxygen binding site is a binuclear iron center. The iron atoms are coordinated to the protein through the carboxylate side chains of a glutamate and aspartate and five histidine residues. The uptake of O 2 by hemerythrin is accompanied by two-electron oxidation of the reduced binuclear center to produce bound peroxide (OOH − ).
'red') is an oligomeric protein responsible for oxygen (O 2) transport in the marine invertebrate phyla of sipunculids, priapulids, brachiopods, and in a single annelid worm genus, Magelona. Myohemerythrin is a monomeric O 2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless ...