Multinuclear blue copper-proteins: the evolutionary design

Abstract

The review presents both our and literature data of results of studies of pathways of evolution of the so-called multinuclear blue copper-proteins (MBCP) that have the domain organization. The MBCP are widely spread in living nature, they have been revealed in cells of archais, bacteria, and eukaryotes. Included in the MBCP composition are such different by their functions copper-proteins as oxidases, reductase, blood coagulation factors V and VIII. Most likely, MBCP have been originated from the low-molecular protein-precursor similar topologically with blue electron-transporting protein of the type of cupredoxin, as a result of action of various evolutionary mechanisms: amplification of genes, formation of protein structures by different combinations of domains, a change of size of domains, the segment elongation at the expense of the activational domain, formation and loss of various copper-binding centres, variation of amino acid ligands in such centres, the appearance of centres of binding of other proteins, glycosylation, etc.