Impact of copper ligand mutations on a cupredoxin with a green copper center

Autores
Roger, Magali; Sciara, Giuliano; Biaso, Frédéric; Lojou, Elisabeth; Wang, Xie; Bauzan, Marielle; Giudici Orticoni, Marie-Thérèse; Vila, Alejandro Jose; Ilbert, Marianne
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and a methionine. The recent discovery of new members of this family with unusual properties demonstrates, however, the versatility of this class of proteins. Changes in their ligand set lead to drastic variation in their metal site geometry and in the resulting spectroscopic and redox features. In our work, we report the identification of the copper ligands in the recently discovered cupredoxin AcoP. We show that even though AcoP possesses a classical copper ligand set, it has a highly perturbed copper center. In depth studies of mutant's properties suggest a high degree of constraint existing in the copper center of the wild type protein and even the addition of exogenous ligands does not lead to the reconstitution of the initial copper center. Not only the chemical nature of the axial ligand but also constraints brought by its covalent binding to the protein backbone might be critical to maintain a green copper site with high redox potential. This work illustrates the importance of experimentally dissecting the molecular diversity of cupredoxins to determine the molecular determinants responsible for their copper center geometry and redox potential.
Fil: Roger, Magali. Aix Marseille Univ; Francia
Fil: Sciara, Giuliano. Aix Marseille Univ; Francia
Fil: Biaso, Frédéric. Aix Marseille Univ; Francia
Fil: Lojou, Elisabeth. Aix Marseille Univ; Francia
Fil: Wang, Xie. Aix Marseille Univ; Francia
Fil: Bauzan, Marielle. Aix Marseille Univ; Francia
Fil: Giudici Orticoni, Marie-Thérèse. Aix Marseille Univ; Francia
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Biológica. Área Biofísica; Argentina
Fil: Ilbert, Marianne. Aix Marseille Univ; Francia
Materia
Acidithiobacillus Ferrooxidans
Copper
Cupredoxin
Green Copper Site
Metal Center
Metalloprotein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/66444
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/66444
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Impact of copper ligand mutations on a cupredoxin with a green copper centerRoger, MagaliSciara, GiulianoBiaso, FrédéricLojou, ElisabethWang, XieBauzan, MarielleGiudici Orticoni, Marie-ThérèseVila, Alejandro JoseIlbert, MarianneAcidithiobacillus FerrooxidansCopperCupredoxinGreen Copper SiteMetal CenterMetalloproteinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and a methionine. The recent discovery of new members of this family with unusual properties demonstrates, however, the versatility of this class of proteins. Changes in their ligand set lead to drastic variation in their metal site geometry and in the resulting spectroscopic and redox features. In our work, we report the identification of the copper ligands in the recently discovered cupredoxin AcoP. We show that even though AcoP possesses a classical copper ligand set, it has a highly perturbed copper center. In depth studies of mutant's properties suggest a high degree of constraint existing in the copper center of the wild type protein and even the addition of exogenous ligands does not lead to the reconstitution of the initial copper center. Not only the chemical nature of the axial ligand but also constraints brought by its covalent binding to the protein backbone might be critical to maintain a green copper site with high redox potential. This work illustrates the importance of experimentally dissecting the molecular diversity of cupredoxins to determine the molecular determinants responsible for their copper center geometry and redox potential.Fil: Roger, Magali. Aix Marseille Univ; FranciaFil: Sciara, Giuliano. Aix Marseille Univ; FranciaFil: Biaso, Frédéric. Aix Marseille Univ; FranciaFil: Lojou, Elisabeth. Aix Marseille Univ; FranciaFil: Wang, Xie. Aix Marseille Univ; FranciaFil: Bauzan, Marielle. Aix Marseille Univ; FranciaFil: Giudici Orticoni, Marie-Thérèse. Aix Marseille Univ; FranciaFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Biológica. Área Biofísica; ArgentinaFil: Ilbert, Marianne. Aix Marseille Univ; FranciaElsevier Science2017-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66444Roger, Magali; Sciara, Giuliano; Biaso, Frédéric; Lojou, Elisabeth; Wang, Xie; et al.; Impact of copper ligand mutations on a cupredoxin with a green copper center; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1858; 5; 5-2017; 351-3590005-2728CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005272817300294info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbabio.2017.02.007info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:30Zoai:ri.conicet.gov.ar:11336/66444instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:45:30.68CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Impact of copper ligand mutations on a cupredoxin with a green copper center
title Impact of copper ligand mutations on a cupredoxin with a green copper center
spellingShingle Impact of copper ligand mutations on a cupredoxin with a green copper center
Roger, Magali
Acidithiobacillus Ferrooxidans
Copper
Cupredoxin
Green Copper Site
Metal Center
Metalloprotein
title_short Impact of copper ligand mutations on a cupredoxin with a green copper center
title_full Impact of copper ligand mutations on a cupredoxin with a green copper center
title_fullStr Impact of copper ligand mutations on a cupredoxin with a green copper center
title_full_unstemmed Impact of copper ligand mutations on a cupredoxin with a green copper center
title_sort Impact of copper ligand mutations on a cupredoxin with a green copper center
dc.creator.none.fl_str_mv Roger, Magali
Sciara, Giuliano
Biaso, Frédéric
Lojou, Elisabeth
Wang, Xie
Bauzan, Marielle
Giudici Orticoni, Marie-Thérèse
Vila, Alejandro Jose
Ilbert, Marianne
author Roger, Magali
author_facet Roger, Magali
Sciara, Giuliano
Biaso, Frédéric
Lojou, Elisabeth
Wang, Xie
Bauzan, Marielle
Giudici Orticoni, Marie-Thérèse
Vila, Alejandro Jose
Ilbert, Marianne
author_role author
author2 Sciara, Giuliano
Biaso, Frédéric
Lojou, Elisabeth
Wang, Xie
Bauzan, Marielle
Giudici Orticoni, Marie-Thérèse
Vila, Alejandro Jose
Ilbert, Marianne
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Acidithiobacillus Ferrooxidans
Copper
Cupredoxin
Green Copper Site
Metal Center
Metalloprotein
topic Acidithiobacillus Ferrooxidans
Copper
Cupredoxin
Green Copper Site
Metal Center
Metalloprotein
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and a methionine. The recent discovery of new members of this family with unusual properties demonstrates, however, the versatility of this class of proteins. Changes in their ligand set lead to drastic variation in their metal site geometry and in the resulting spectroscopic and redox features. In our work, we report the identification of the copper ligands in the recently discovered cupredoxin AcoP. We show that even though AcoP possesses a classical copper ligand set, it has a highly perturbed copper center. In depth studies of mutant's properties suggest a high degree of constraint existing in the copper center of the wild type protein and even the addition of exogenous ligands does not lead to the reconstitution of the initial copper center. Not only the chemical nature of the axial ligand but also constraints brought by its covalent binding to the protein backbone might be critical to maintain a green copper site with high redox potential. This work illustrates the importance of experimentally dissecting the molecular diversity of cupredoxins to determine the molecular determinants responsible for their copper center geometry and redox potential.
Fil: Roger, Magali. Aix Marseille Univ; Francia
Fil: Sciara, Giuliano. Aix Marseille Univ; Francia
Fil: Biaso, Frédéric. Aix Marseille Univ; Francia
Fil: Lojou, Elisabeth. Aix Marseille Univ; Francia
Fil: Wang, Xie. Aix Marseille Univ; Francia
Fil: Bauzan, Marielle. Aix Marseille Univ; Francia
Fil: Giudici Orticoni, Marie-Thérèse. Aix Marseille Univ; Francia
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Biológica. Área Biofísica; Argentina
Fil: Ilbert, Marianne. Aix Marseille Univ; Francia
description Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and a methionine. The recent discovery of new members of this family with unusual properties demonstrates, however, the versatility of this class of proteins. Changes in their ligand set lead to drastic variation in their metal site geometry and in the resulting spectroscopic and redox features. In our work, we report the identification of the copper ligands in the recently discovered cupredoxin AcoP. We show that even though AcoP possesses a classical copper ligand set, it has a highly perturbed copper center. In depth studies of mutant's properties suggest a high degree of constraint existing in the copper center of the wild type protein and even the addition of exogenous ligands does not lead to the reconstitution of the initial copper center. Not only the chemical nature of the axial ligand but also constraints brought by its covalent binding to the protein backbone might be critical to maintain a green copper site with high redox potential. This work illustrates the importance of experimentally dissecting the molecular diversity of cupredoxins to determine the molecular determinants responsible for their copper center geometry and redox potential.
publishDate 2017
dc.date.none.fl_str_mv 2017-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/66444
Roger, Magali; Sciara, Giuliano; Biaso, Frédéric; Lojou, Elisabeth; Wang, Xie; et al.; Impact of copper ligand mutations on a cupredoxin with a green copper center; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1858; 5; 5-2017; 351-359
0005-2728
CONICET Digital
CONICET
url http://hdl.handle.net/11336/66444
identifier_str_mv Roger, Magali; Sciara, Giuliano; Biaso, Frédéric; Lojou, Elisabeth; Wang, Xie; et al.; Impact of copper ligand mutations on a cupredoxin with a green copper center; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1858; 5; 5-2017; 351-359
0005-2728
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005272817300294
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbabio.2017.02.007
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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