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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Detalles Bibliográficos
Autores principales: Szuster, Jonathan, Zitare, Ulises A., Castro, María A., Leguto, Alcides J., Morgada, Marcos Nicolás, Vila, Alejandro J., Murgida, Daniel H.
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Royal Society of Chemistry 2021
Materias:
Copper
Metalloproteins
Oxidation-Reduction
Ligands
Acceso en línea:http://hdl.handle.net/2133/20481
http://hdl.handle.net/2133/20481
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-20481
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
topic Copper
Metalloproteins
Oxidation-Reduction
Ligands
spellingShingle Copper
Metalloproteins
Oxidation-Reduction
Ligands
Szuster, Jonathan
Zitare, Ulises A.
Castro, María A.
Leguto, Alcides J.
Morgada, Marcos Nicolás
Vila, Alejandro J.
Murgida, Daniel H.
CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
topic_facet Copper
Metalloproteins
Oxidation-Reduction
Ligands
description 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
format article
artículo
publishedVersion
author Szuster, Jonathan
Zitare, Ulises A.
Castro, María A.
Leguto, Alcides J.
Morgada, Marcos Nicolás
Vila, Alejandro J.
Murgida, Daniel H.
author_facet Szuster, Jonathan
Zitare, Ulises A.
Castro, María A.
Leguto, Alcides J.
Morgada, Marcos Nicolás
Vila, Alejandro J.
Murgida, Daniel H.
author_sort Szuster, Jonathan
title CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
title_short CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
title_full CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
title_fullStr CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
title_full_unstemmed CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
title_sort cua-based chimeric t1 copper sites allow for independent modulation of reorganization energy and reduction potential
publisher Royal Society of Chemistry
publishDate 2021
url http://hdl.handle.net/2133/20481
http://hdl.handle.net/2133/20481
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