The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase

Autores
Cerqueira, Nuno M. F. S. A.; Fernandes, Pedro A.; González, Pablo Javier; Moura, José J. G.; Ramos, Maria J.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A structural rearrangement known as sulfur shift occurs in some Mo-containing enzymes of the DMSO reductase family. This mechanism is characterized by the displacement of a coordinating cysteine thiol (or SeCys in Fdh) from the first to the second shell of the Mo-coordination sphere metal. The hexa-coordinated Mo ion found in the as-isolated state cannot bind directly any exogenous ligand (substrate or inhibitors), while the penta-coordinated ion, attained upon sulfur shift, has a free binding site for direct coordination of the substrate. This rearrangement provides an efficient mechanism to keep a constant coordination number throughout an entire catalytic pathway. This mechanism is very similar to the carboxylate shift observed in Zn-dependent enzymes, and it has been recently detected by experimental means. In the present paper, we calculated the geometries and energies involved in the sulfur-shift mechanism using QM-methods (M06/(6-311++G(3df,2pd),SDD)//B3LYP/(6-31G(d),SDD)). The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination.
Fil: Cerqueira, Nuno M. F. S. A.. Universidad de Porto; Portugal
Fil: Fernandes, Pedro A.. Universidad de Porto; Portugal
Fil: González, Pablo Javier. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; Argentina
Fil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; Portugal
Fil: Ramos, Maria J.. Universidad de Porto; Portugal
Materia
Molybdenum
Sulfur-Shift
Nitrate Reductase
Formate Dehydrogenase
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:11336/6501
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate DehydrogenaseCerqueira, Nuno M. F. S. A.Fernandes, Pedro A.González, Pablo JavierMoura, José J. G.Ramos, Maria J.MolybdenumSulfur-ShiftNitrate ReductaseFormate Dehydrogenasehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A structural rearrangement known as sulfur shift occurs in some Mo-containing enzymes of the DMSO reductase family. This mechanism is characterized by the displacement of a coordinating cysteine thiol (or SeCys in Fdh) from the first to the second shell of the Mo-coordination sphere metal. The hexa-coordinated Mo ion found in the as-isolated state cannot bind directly any exogenous ligand (substrate or inhibitors), while the penta-coordinated ion, attained upon sulfur shift, has a free binding site for direct coordination of the substrate. This rearrangement provides an efficient mechanism to keep a constant coordination number throughout an entire catalytic pathway. This mechanism is very similar to the carboxylate shift observed in Zn-dependent enzymes, and it has been recently detected by experimental means. In the present paper, we calculated the geometries and energies involved in the sulfur-shift mechanism using QM-methods (M06/(6-311++G(3df,2pd),SDD)//B3LYP/(6-31G(d),SDD)). The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination.Fil: Cerqueira, Nuno M. F. S. A.. Universidad de Porto; PortugalFil: Fernandes, Pedro A.. Universidad de Porto; PortugalFil: González, Pablo Javier. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; ArgentinaFil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; PortugalFil: Ramos, Maria J.. Universidad de Porto; PortugalAmerican Chemical Society2013-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/6501Cerqueira, Nuno M. F. S. A.; Fernandes, Pedro A.; González, Pablo Javier; Moura, José J. G.; Ramos, Maria J.; The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase; American Chemical Society; Inorganic Chemistry; 52; 19; 9-2013; 10766-107720020-1669enginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ic3028034info:eu-repo/semantics/altIdentifier/doi/10.1021/ic3028034info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:40:10Zoai:ri.conicet.gov.ar:11336/6501instacron: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:34982025-09-29 10:40:10.437CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
title The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
spellingShingle The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
Cerqueira, Nuno M. F. S. A.
Molybdenum
Sulfur-Shift
Nitrate Reductase
Formate Dehydrogenase
title_short The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
title_full The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
title_fullStr The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
title_full_unstemmed The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
title_sort The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
dc.creator.none.fl_str_mv Cerqueira, Nuno M. F. S. A.
Fernandes, Pedro A.
González, Pablo Javier
Moura, José J. G.
Ramos, Maria J.
author Cerqueira, Nuno M. F. S. A.
author_facet Cerqueira, Nuno M. F. S. A.
Fernandes, Pedro A.
González, Pablo Javier
Moura, José J. G.
Ramos, Maria J.
author_role author
author2 Fernandes, Pedro A.
González, Pablo Javier
Moura, José J. G.
Ramos, Maria J.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Molybdenum
Sulfur-Shift
Nitrate Reductase
Formate Dehydrogenase
topic Molybdenum
Sulfur-Shift
Nitrate Reductase
Formate Dehydrogenase
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A structural rearrangement known as sulfur shift occurs in some Mo-containing enzymes of the DMSO reductase family. This mechanism is characterized by the displacement of a coordinating cysteine thiol (or SeCys in Fdh) from the first to the second shell of the Mo-coordination sphere metal. The hexa-coordinated Mo ion found in the as-isolated state cannot bind directly any exogenous ligand (substrate or inhibitors), while the penta-coordinated ion, attained upon sulfur shift, has a free binding site for direct coordination of the substrate. This rearrangement provides an efficient mechanism to keep a constant coordination number throughout an entire catalytic pathway. This mechanism is very similar to the carboxylate shift observed in Zn-dependent enzymes, and it has been recently detected by experimental means. In the present paper, we calculated the geometries and energies involved in the sulfur-shift mechanism using QM-methods (M06/(6-311++G(3df,2pd),SDD)//B3LYP/(6-31G(d),SDD)). The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination.
Fil: Cerqueira, Nuno M. F. S. A.. Universidad de Porto; Portugal
Fil: Fernandes, Pedro A.. Universidad de Porto; Portugal
Fil: González, Pablo Javier. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe; Argentina
Fil: Moura, José J. G.. Universidade Nova de Lisboa. Faculdade de Ciencias e Tecnologia. Departamento de Química; Portugal
Fil: Ramos, Maria J.. Universidad de Porto; Portugal
description A structural rearrangement known as sulfur shift occurs in some Mo-containing enzymes of the DMSO reductase family. This mechanism is characterized by the displacement of a coordinating cysteine thiol (or SeCys in Fdh) from the first to the second shell of the Mo-coordination sphere metal. The hexa-coordinated Mo ion found in the as-isolated state cannot bind directly any exogenous ligand (substrate or inhibitors), while the penta-coordinated ion, attained upon sulfur shift, has a free binding site for direct coordination of the substrate. This rearrangement provides an efficient mechanism to keep a constant coordination number throughout an entire catalytic pathway. This mechanism is very similar to the carboxylate shift observed in Zn-dependent enzymes, and it has been recently detected by experimental means. In the present paper, we calculated the geometries and energies involved in the sulfur-shift mechanism using QM-methods (M06/(6-311++G(3df,2pd),SDD)//B3LYP/(6-31G(d),SDD)). The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination.
publishDate 2013
dc.date.none.fl_str_mv 2013-09
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/11336/6501
Cerqueira, Nuno M. F. S. A.; Fernandes, Pedro A.; González, Pablo Javier; Moura, José J. G.; Ramos, Maria J.; The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase; American Chemical Society; Inorganic Chemistry; 52; 19; 9-2013; 10766-10772
0020-1669
url http://hdl.handle.net/11336/6501
identifier_str_mv Cerqueira, Nuno M. F. S. A.; Fernandes, Pedro A.; González, Pablo Javier; Moura, José J. G.; Ramos, Maria J.; The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase; American Chemical Society; Inorganic Chemistry; 52; 19; 9-2013; 10766-10772
0020-1669
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ic3028034
info:eu-repo/semantics/altIdentifier/doi/10.1021/ic3028034
info:eu-repo/semantics/altIdentifier/doi/
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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 13.070432

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