Abstract
The imidazole side chain of the copper-coordinating histidine 117 of the type-1 copper protein Pseudomonas aeruginosa azurin protrudes through the surface of the proteins where it has contact with the solvent. Replacement of this histidine by a glycine, using site-directed mutagenesis, makes the copper center amenable to direct manipulation through the addition of external ligands. Depending on the kind of the externally added ligand, different type-1 and type-2 copper centers are obtained with UV/vis and EPR spectroscopic characteristics that encompass the known range of proteins with one copper in their active sites
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