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• W1936006951 endingPage "3129" @default.
• W1936006951 startingPage "3123" @default.
• W1936006951 abstract "Azurin contains two potential redox sites, a copper centre and, at the opposite end of the molecule, a cystine disulfide (RSSR). Intramolecular electron transfer between a pulse radiolytically produced RSSR− radical anion and the blue Cu(II) ion was studied in a series of azurins in which single-site mutations were introduced into the copper ligand sphere. In the Met121His mutant, the rate constant for intramolecular electron transfer is half that of the corresponding wild-type azurin. In the His46Gly and His117Gly mutants, a water molecule is co-ordinated to the copper ion when no external ligands are added. Both these mutants also exhibit slower intramolecular electron transfer than the corresponding wild-type azurin. However, for the His117Gly mutant in the presence of excess imidazole, an azurin–imidazole complex is formed and the intramolecular electron-transfer rate increases considerably, becoming threefold faster than that observed in the native protein. Activation parameters for all these electron-transfer processes were determined and combined with data from earlier studies on intramolecular electron transfer in wild-type and single-site-mutated azurins. A linear relationship between activation enthalpy and activation entropy was observed. These results are discussed in terms of reorganization energies, driving force and possible electron-transfer pathways." @default.
• W1936006951 created "2016-06-24" @default.
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• W1936006951 date "2000-06-01" @default.
• W1936006951 modified "2023-10-10" @default.
• W1936006951 title "Role of ligand substitution on long-range electron transfer in azurins" @default.
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• W1936006951 doi "https://doi.org/10.1046/j.1432-1327.2000.01317.x" @default.
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