Ceruloplasmin catalytic activity

The phylogenetic paths of plants and animals diverged approximately 1.4 billion years ago, leading to laccase and ascorbate oxidase in the former group, and ceruloplasmin in the latter. Then, 500-800 million years ago, the coagulation factors CF5 and CF8 were created from the precursor of present day ceruloplasmin. This included the loss of the copper centers and, consequently, their catalytic activity [71]. 

Copper is also necessary for the efficient utilisation of iron and for the biosynthesis of some physiologically important compounds, such as the enzyme ceruloplasmin, which is produced in Hver cells and acts in the blood plasma as the main Cu compound, but it is not involved in copper transport to the target organs. Plasma copper is transported primarily bound to albumin and partly in the form of complexes with low molecular weight ligands, such as histidine. Ceruloplasmin also has the catalytic activity of ferro oxidase, which means that it catalyses the oxidation of Fe " " ions absorbed in the blood plasma to Fe + ions, thus allowing fixation of iron in the transferrin molecule. Copper deficiency, therefore, is similar to iron deficiency and leads to anaemia. 

Catalytic reduction of oxygen directly to water, while not as yet possible with traditional catalyst technology at neutral pH, is achieved with some biocatalysts, particularly by enzymes with multi-copper active sites such as the laccases, ceruloplasmins, ascorbate oxidase and bilirubin oxidases. The first report on the use of a biocatalyst... 

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