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Oxygen transportation, DNA synthesis, myelin synthesis, oxidative phosphorylation, and neurotransmitter synthesis and metabolism are all biological processes that require iron; however, an iron imbalance can result in neurotoxicity causing oxidation and modification of lipids, proteins, carbohydrates, and DNA. [31]
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.
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 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.
Finally, although mineral and elements are in many ways synonymous, minerals are only bioavailable to the extent that they can be absorbed. To be absorbed, minerals either must be soluble or readily extractable by the consuming organism. For example, molybdenum is an essential mineral, but metallic molybdenum has no nutritional benefit.
Hemocyanin oxygen-binding profile is also affected by dissolved salt ion levels and pH. [14] Hemocyanin is made of many individual subunit proteins, each of which contains two copper atoms and can bind one oxygen molecule (O 2). Each subunit weighs about 75 kilodaltons (kDa).
In physiology, respiration is the transport of oxygen from the outside environment to the cells within tissues, and the removal of carbon dioxide in the opposite direction to the environment by a respiratory system.
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 − ).