Blue Copper Proteins

Blue copper proteins were first isolated from bacteria in the 1950s and from plant tissues in the early 1960s. The intense blue color of these proteins is due to a strong absorption band at a wavelength of about 600 nm. Although simple Cu²⁺ complexes, such as [Cu(H₂O)₆]²⁺ and [Cu(NH₃)₄]²⁺, are also blue due to an absorption band at 600 nm, the intensity of the absorption band is about 100 times less than that of a blue copper protein. Moreover, the reduction potential for the Cu²⁺/Cu⁺ couple in a blue copper protein is usually +0.3 to +0.5 V, considerably more positive than that of the aqueous Cu²⁺/Cu⁺ couple (+0.15 V).

Figure 1.1

: A Blue Copper Protein. In both the oxidized and reduced forms of a blue copper protein, the copper is coordinated by four ligands (two histidine imidazole nitrogen atoms, a cysteine thiolate sulfur, and a thioether sulfur of a methionine) in a roughly tetrahedral arrangement.

The copper center in blue copper proteins has a distorted tetrahedral structure, in which the copper is bound to four amino acid side chains (Figure 1.1). Although the most common structures for four-coordinate Cu²⁺ and Cu⁺ complexes are square planar and tetrahedral, respectively, the structures of the oxidized (Cu²⁺) and reduced (Cu⁺) forms of the protein are essentially identical. Thus the protein forces the Cu²⁺ ion to adopt a higher-energy structure that is more suitable for Cu⁺, which makes the Cu²⁺ form easier to reduce and raises its reduction potential.