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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/6501
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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 Técnicas2025-09-03T10:09:32Zoai: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:34982025-09-03 10:09:32.485CONICET 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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 |