CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
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Royal Society of Chemistry
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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 CuA protein leads to a series
of distorted T1-like sites that allow for independent modulation of reduction potentials (E°´) and electron
transfer reorganization energies (l). On the one hand E°´ values could be fine-tuned over 120 mV
without affecting l. On the other, l 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
Para citar este articulo: Chem. Sci., 2020, 11, 6193
Para citar este articulo: Chem. Sci., 2020, 11, 6193
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