Charge effect in protein metalation reactions by diruthenium complexes

The properties of paddlewheel diruthenium compounds significantly depend on the nature of the bridging equatorial ligands. The charge of these complexes is a factor to take into account when studying their interaction with proteins. To compare the reactivity of diruthenium compounds with the model p...

Descripción completa

Detalles Bibliográficos
Autores: Terán More, Aaron, Ferraro, Giarita, Sánchez-Peláez, Ana, Herrero Domínguez, Santiago, Merlino, Antonello
Tipo de recurso: artículo
Fecha de publicación:2023
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/88176
Acceso en línea:https://hdl.handle.net/20.500.14352/88176
Access Level:acceso abierto
Palabra clave:Cristalografía (Química)
2303 Química Inorgánica
id ES_15e00aec539d11a3b6cfdc8626990e51
oai_identifier_str oai:docta.ucm.es:20.500.14352/88176
network_acronym_str ES
network_name_str España
repository_id_str
spelling Charge effect in protein metalation reactions by diruthenium complexesTerán More, AaronFerraro, GiaritaSánchez-Peláez, AnaHerrero Domínguez, SantiagoMerlino, AntonelloCristalografía (Química)2303 Química InorgánicaThe properties of paddlewheel diruthenium compounds significantly depend on the nature of the bridging equatorial ligands. The charge of these complexes is a factor to take into account when studying their interaction with proteins. To compare the reactivity of diruthenium compounds with the model protein hen egg white lysozyme (HEWL), we have prepared the well-known anionic complex [Ru2(CO3)4]3−, two new anionic species, [Ru2(D-p-FPhF)(CO3)3]2− and [Ru2(DAniF)(CO3)3]2−, and their analogues [Ru2Cl(D-p-FPhF)(O2CCH3)3] and [Ru2Cl(DAniF)(O2CCH3)3] that generate cationic species in solution (D-p-FPhF− = N,N′-bis(4-fluorophenyl)formamidinate and DAniF− = N,N′-bis(4-methoxyphenyl)formamidinate). The interaction of these compounds with HEWL was investigated by UV-vis absorption spectroscopy, circular dichroism, intrinsic fluorescence and X-ray crystallography. The molecular structures of the adducts differ in the number of metal binding sites, in the binding mode and in the type of fragments that are bound to the protein. The charge of the diruthenium complexes in aqueous solutions strongly influences their protein binding properties. High-negative charge complexes are non-covalently bound. However, the replacement of carbonate ligands changes the negative charge of these complexes and favours covalent binding. These results have great implications for further studies in the tailoring of artificial diruthenium-containing metalloenzymes.Royal Society of ChemistryUniversidad Complutense de Madrid20232023-01-0120232023-01-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/88176reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/881762026-06-02T12:44:21Z
dc.title.none.fl_str_mv Charge effect in protein metalation reactions by diruthenium complexes
title Charge effect in protein metalation reactions by diruthenium complexes
spellingShingle Charge effect in protein metalation reactions by diruthenium complexes
Terán More, Aaron
Cristalografía (Química)
2303 Química Inorgánica
title_short Charge effect in protein metalation reactions by diruthenium complexes
title_full Charge effect in protein metalation reactions by diruthenium complexes
title_fullStr Charge effect in protein metalation reactions by diruthenium complexes
title_full_unstemmed Charge effect in protein metalation reactions by diruthenium complexes
title_sort Charge effect in protein metalation reactions by diruthenium complexes
dc.creator.none.fl_str_mv Terán More, Aaron
Ferraro, Giarita
Sánchez-Peláez, Ana
Herrero Domínguez, Santiago
Merlino, Antonello
author Terán More, Aaron
author_facet Terán More, Aaron
Ferraro, Giarita
Sánchez-Peláez, Ana
Herrero Domínguez, Santiago
Merlino, Antonello
author_role author
author2 Ferraro, Giarita
Sánchez-Peláez, Ana
Herrero Domínguez, Santiago
Merlino, Antonello
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv Cristalografía (Química)
2303 Química Inorgánica
topic Cristalografía (Química)
2303 Química Inorgánica
description The properties of paddlewheel diruthenium compounds significantly depend on the nature of the bridging equatorial ligands. The charge of these complexes is a factor to take into account when studying their interaction with proteins. To compare the reactivity of diruthenium compounds with the model protein hen egg white lysozyme (HEWL), we have prepared the well-known anionic complex [Ru2(CO3)4]3−, two new anionic species, [Ru2(D-p-FPhF)(CO3)3]2− and [Ru2(DAniF)(CO3)3]2−, and their analogues [Ru2Cl(D-p-FPhF)(O2CCH3)3] and [Ru2Cl(DAniF)(O2CCH3)3] that generate cationic species in solution (D-p-FPhF− = N,N′-bis(4-fluorophenyl)formamidinate and DAniF− = N,N′-bis(4-methoxyphenyl)formamidinate). The interaction of these compounds with HEWL was investigated by UV-vis absorption spectroscopy, circular dichroism, intrinsic fluorescence and X-ray crystallography. The molecular structures of the adducts differ in the number of metal binding sites, in the binding mode and in the type of fragments that are bound to the protein. The charge of the diruthenium complexes in aqueous solutions strongly influences their protein binding properties. High-negative charge complexes are non-covalently bound. However, the replacement of carbonate ligands changes the negative charge of these complexes and favours covalent binding. These results have great implications for further studies in the tailoring of artificial diruthenium-containing metalloenzymes.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023-01-01
2023
2023-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/88176
url https://hdl.handle.net/20.500.14352/88176
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869403820594823168
score 15,300719

Similares en LA Referencia