Tuning reduction potentials of type 1 copper center in azurin by replacing a histidine ligand with its isostructural analogues

• Published in: Journal of inorganic biochemistry Vol. 234; p. 111863
• Main Authors: Yu, Yang, Marshall, Nicholas M., Garner, Dewain K., Nilges, Mark J., Lu, Yi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2022
• Subjects: Blue copper; Cupredoxins; Electron transfer; Protein engineering; Redox; Unnatural amino acids; Redox; Blue copper; Electron transfer; Protein engineering; Cupredoxins; Unnatural amino acids

Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine. While the cysteine and methionine in azurin have been replaced with their respective isostructural analogues of unnatural amino acids to rev...