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We replaced a copper\u2010coordinating histidine (His) in the active site of the redox enzyme azurin with exogenous dimethyl imidazolylidene. This NHC rapidly restores the type\u20101 Cu center, with spectroscopic properties (EPR, UV\/Vis) that are identical to those from N\u2010coordination of the His in the wild type. However, the introduction of the NHC markedly alters the redox potential of the metal, which is a key functionality of this blue copper protein. 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