Blue copper proteins metal substitution

A keyword search will provide access to coordinate sets from all species that are currently available as well as various site-directed mutants, type 1 copper proteins substituted with metals other than copper, and ruthenated blue copper protein derivatives. Table 1 provides a summary (with references) of the structures of blue copper-binding domains elucidated using X-ray crystallography and NMR spectroscopy. 

Another problem with small models is that molecules from the solution (e.g. water) may come in and stabilise tetragonal structures and higher coordination numbers [224]. It is illustrative that very few inorganic con5)lexes reproduce the properties of the blue copper proteins [66,67], whereas typical blue-copper sites have been constructed in several proteins and peptides by metal substitution, e.g. insulin, alcohol dehydrogenase, and superoxide dismutase [66]. This shows that the problem is more related to protection from water and dimer formation than to strain. 

Many (although not all) spectroscopic data on metal-substituted derivatives and their binary and ternary complexes have also been interpreted as indicative of a four-coordinate metal.Even nickel(II) and copper(II), which have little tendency to adapt to a pseudotetrahedral ligand environment, do so in LADH, the electronic structure of the latter resembling that of blue proteins (Figure 2.36). ... 

A remarkable feature of blue, green, and purple cupredoxins is that very little structural change is observed upon reduction. In the case of the blue and green copper centers, the same observation holds true for proteins when the copper ion is removed, or is substituted by a variety of other metal ions (such as Hg°, Co°, and Zn°) with totally different preferences for coordination geometry and ligand donor sets. 

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