Iron-containing proteins mammalian transferrin

Spectroscopic data obtained from spectroelectrochemical experiments require careful and case-specific analysis. The Fe /Fe redox couple has a unique role in diflferent iron-containing proteins. It is hypothesised that the mammalian iron-transport protein transferrin uses the Fe /Fe redox couple as a switch that controls the time and site-specific release of iron, while other iron-containing proteins, such as myoglobin, are able to hold on to iron in both oxidation states. Therefore, it is very important to evaluate the protein and its interaction with both the oxidised and reduced states of iron and accordingly develop a data-analysis model. The spectroelectrochemical response of an iron binding protein can be ideal Nernstian, non-Nernstian resulting from coupled... 

Ceruloplasmin is an intensely blue glycoprotein of the a2-globulin fraction of mammalian blood, which acts as a copper transfer protein and probably has a role in iron storage. The structure is known it contains three Type 1 (Tl) sites (one of which seems to be inactive) and a Type 2/Type 3 (T2/T3) trinuclear cluster. It is believed to be part of the process of oxidizing Fe(II) to Fe(III) in the transfer of iron from ferritin to transferrin. Reduction of two Tl sites and the T3 pair is fast, but reduction of the T2 Cu site is slow the pathways of electron transfer between the sites have been investigated, but the complete mechanism is still unknown. 

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