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Ferroportin-mediated iron efflux is calcium-activated; studies of human Fpn expressed in Xenopus laevis oocytes demonstrated that calcium is a required cofactor for Fpn, but that Fpn does not transport calcium. [12] Thus, Fpn does not function as an iron/calcium antiporter. The thermodynamic driving force for Fpn remains unknown.
However, some of the intracellular iron is bound to low-affinity complexes, and is termed labile iron or "free" iron. Iron in such complexes can cause damage as described above. [2] To prevent that kind of damage, all life forms that use iron bind the iron atoms to proteins. This binding allows cells to benefit from iron while also limiting its ...
ATP, the main source of energy in almost all living organisms, must bind with metal ions such as Mg 2+ or Ca 2+ to function. Examination of cells with limited magnesium supply has shown that a lack of magnesium can cause a decrease in ATP. [9] Magnesium in ATP hydrolysis acts as a co-factor to stabilize the high negative charge transition state ...
The coordination sphere of the calcium ion contains only carboxylate oxygen atoms and no nitrogen atoms. This is consistent with the hard nature of the calcium ion. The protein has two approximately symmetrical domains, separated by a flexible "hinge" region. Binding of calcium causes a conformational change to occur in the protein.
In hemoglobin, the iron is in one of four heme groups and has six possible coordination sites; four are occupied by nitrogen atoms in a porphyrin ring, the fifth by an imidazole nitrogen in a histidine residue of one of the protein chains attached to the heme group, and the sixth is reserved for the oxygen molecule it can reversibly bind to. [5]
The oxygen binds to the iron in the heme via affinity-based binding or liganding and dissociates from the protein once it has reached its destination. [14] Iron can also be a potential carcinogen in three ways; first being the production of hydroxyl radicals .