CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential.
Chem Sci
; 11(24): 6193-6201, 2020 Jun 28.
Article
em En
| MEDLINE
| ID: mdl-32953013
ABSTRACT
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 (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.
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01-internacional
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MEDLINE
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article