Metalloproteins stellacyanin

Stellacyanin, the plastocyanins, and the azurins are the most widely studied copper-containing metalloproteins of the next active-site class, the Blue Copper sites. These proteins, which generally appear to be involved in redox chemistry, have quite unique spectral features32,33). The potential for complementary interaction between inorganic spectroscopy and protein crystallography is well demonstrated by the roles that they have played in generating fairly detailed geometric and electronic structural pictures of the Blue Copper metal centers. 

The electrochemical methods discussed above have been used to study ET in a variety of other metalloproteins [2, 3, 15, 60, 61] including cytochrome [15], stellacyanin [15], and multicopper enzymes [3]. DNA bases have also been found to participate and mediate ET [62], in analogy to the results found for proteins. Charge transfer in DNA is thought to be fundamental in DNA oxidative processes, like oxidative damage and its repair [63]. Thus, ET in DNA offers interesting opportunities for fundamental research and technological applications. The field has experienced intensive research in the last years and has been recently reviewed in [63, 64]. 

Structural studies on electron transfer metalloproteins provide an important origin for discussion of the electron transfer processes themselves.The reduction potentials of a number of cytochromes c, cyt c copper blue proteins plastocyanin, Pc azurin, Az stellacyanin, St and HiPIP, or high potential iron protein, from Chromatium vinosum have been determined using spectro-... 

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