Stellacyanin is a protein specific to plants that contains a singular copper ion bound in a blue configuration (type 1). Stellacyanin’s spectroscopic properties help us differentiate it from plastocyanin, which is another monocopper blue protein found in plants. [1]
Stellacyanins are characterized by their uniquely low redox potentials, as low as +180 mv and reach up to 280 mV. Other blue copper protein redox potentials start around 310 mV and reach up to 680 mV. [1]
A mutant cucumber stellacyanin was created by replacing the glutamine axial ligand (a ligand which all other blue proteins contain) with a methionine (Q99M) and purified. The spectroscopic properties found were common to uclacyanin- not plantacyanins. Stellacyanin with the substation of the axial G redox potential was calculated to be +420 mV, which much higher than the redox potential of the stellacyanin found in nature (without methionine) at +260 mV. Structural design also poses the question if stellacyanins may possibly not be diffusible electron transfer proteins in long range electron-transfering. Stellacyanins are most involved in redox reactions of plants that take place during a defense response, and formation of lignin.[1]
Stellacyanins are also distinguishable from plantacyanins and other cupredoxins by the structure if their amino acid residue position relative to the pivotal site of copper.[1]
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