CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
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 le...
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| Autores principales: | , , , , , , |
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| Formato: | article artículo publishedVersion |
| Lenguaje: | Inglés |
| Publicado: |
Royal Society of Chemistry
2021
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/2133/20481 http://hdl.handle.net/2133/20481 |
| Aporte de: |
| Sumario: | 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 |
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