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Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new or improved redox functions. Here we report that implantation of ligand loops from natural T1 proteins into the scaffold of a Cu A protein leads to a series of distorted T1-like sites that allow for independent modulation of reduction potentials ( E °') and electron transfer reorganization energies ( λ ). On the one hand E °' values could be fine-tuned over 120 mV without affecting λ . On the other, λ values could be modulated by more than a factor of two while affecting E °' only by a few millivolts. These results are in sharp contrast to previous studies that used T1 cupredoxin folds, thus highlighting the importance of the protein scaffold in determining such parameters.

CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential

Cu_A-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential