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Cu(A)-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 Cu(A) protein le...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7480511/ https://www.ncbi.nlm.nih.gov/pubmed/32953013 http://dx.doi.org/10.1039/d0sc01620a |
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author | Szuster, Jonathan Zitare, Ulises A. Castro, María A. Leguto, Alcides J. Morgada, Marcos N. Vila, Alejandro J. Murgida, Daniel H. |
author_facet | Szuster, Jonathan Zitare, Ulises A. Castro, María A. Leguto, Alcides J. Morgada, Marcos N. Vila, Alejandro J. Murgida, Daniel H. |
author_sort | Szuster, Jonathan |
collection | PubMed |
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 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. |
format | Online Article Text |
id | pubmed-7480511 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-74805112020-09-18 Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential Szuster, Jonathan Zitare, Ulises A. Castro, María A. Leguto, Alcides J. Morgada, Marcos N. Vila, Alejandro J. Murgida, Daniel H. Chem Sci Chemistry 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. Royal Society of Chemistry 2020-06-01 /pmc/articles/PMC7480511/ /pubmed/32953013 http://dx.doi.org/10.1039/d0sc01620a Text en This journal is © The Royal Society of Chemistry 2020 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0) |
spellingShingle | Chemistry Szuster, Jonathan Zitare, Ulises A. Castro, María A. Leguto, Alcides J. Morgada, Marcos N. Vila, Alejandro J. Murgida, Daniel H. Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential |
title | Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
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title_full | Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
|
title_fullStr | Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
|
title_full_unstemmed | Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
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title_short | Cu(A)-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
|
title_sort | cu(a)-based chimeric t1 copper sites allow for independent modulation of reorganization energy and reduction potential |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7480511/ https://www.ncbi.nlm.nih.gov/pubmed/32953013 http://dx.doi.org/10.1039/d0sc01620a |
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