Substrate binding to a nitrite reductase induces a spin transition
- Autores
- Martins, Gabriel; Rodrigues, Luisa; Cunha, Filipa M.; Matos, Daniela; Hildebrandt, Peter; Murgida, Daniel Horacio; Pereira, Inês A. C.; Todorovic, Smilja
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society.
Fil: Martins, Gabriel. Universidade Nova de Lisboa; Portugal
Fil: Rodrigues, Luisa. Universidade Nova de Lisboa; Portugal. Instituto Gulbenkian de Ciencia; Portugal
Fil: Cunha, Filipa M.. Universidade Nova de Lisboa; Portugal
Fil: Matos, Daniela. Universidade Nova de Lisboa; Portugal
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina
Fil: Pereira, Inês A. C.. Universidade Nova de Lisboa; Portugal
Fil: Todorovic, Smilja. Universidade Nova de Lisboa; Portugal - Materia
-
Nitrite Reductase
Raman - 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:11336/71945
Ver los metadatos del registro completo
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Substrate binding to a nitrite reductase induces a spin transitionMartins, GabrielRodrigues, LuisaCunha, Filipa M.Matos, DanielaHildebrandt, PeterMurgida, Daniel HoracioPereira, Inês A. C.Todorovic, SmiljaNitrite ReductaseRamanhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society.Fil: Martins, Gabriel. Universidade Nova de Lisboa; PortugalFil: Rodrigues, Luisa. Universidade Nova de Lisboa; Portugal. Instituto Gulbenkian de Ciencia; PortugalFil: Cunha, Filipa M.. Universidade Nova de Lisboa; PortugalFil: Matos, Daniela. Universidade Nova de Lisboa; PortugalFil: Hildebrandt, Peter. Technishe Universitat Berlin; AlemaniaFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; ArgentinaFil: Pereira, Inês A. C.. Universidade Nova de Lisboa; PortugalFil: Todorovic, Smilja. Universidade Nova de Lisboa; PortugalAmerican Chemical Society2010-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/71945Martins, Gabriel; Rodrigues, Luisa; Cunha, Filipa M.; Matos, Daniela; Hildebrandt, Peter; et al.; Substrate binding to a nitrite reductase induces a spin transition; American Chemical Society; Journal of Physical Chemistry B; 114; 16; 4-2010; 5563-55661520-6106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jp9118502info:eu-repo/semantics/altIdentifier/doi/10.1021/jp9118502info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:46:32Zoai:ri.conicet.gov.ar:11336/71945instacron: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 09:46:32.857CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Substrate binding to a nitrite reductase induces a spin transition |
title |
Substrate binding to a nitrite reductase induces a spin transition |
spellingShingle |
Substrate binding to a nitrite reductase induces a spin transition Martins, Gabriel Nitrite Reductase Raman |
title_short |
Substrate binding to a nitrite reductase induces a spin transition |
title_full |
Substrate binding to a nitrite reductase induces a spin transition |
title_fullStr |
Substrate binding to a nitrite reductase induces a spin transition |
title_full_unstemmed |
Substrate binding to a nitrite reductase induces a spin transition |
title_sort |
Substrate binding to a nitrite reductase induces a spin transition |
dc.creator.none.fl_str_mv |
Martins, Gabriel Rodrigues, Luisa Cunha, Filipa M. Matos, Daniela Hildebrandt, Peter Murgida, Daniel Horacio Pereira, Inês A. C. Todorovic, Smilja |
author |
Martins, Gabriel |
author_facet |
Martins, Gabriel Rodrigues, Luisa Cunha, Filipa M. Matos, Daniela Hildebrandt, Peter Murgida, Daniel Horacio Pereira, Inês A. C. Todorovic, Smilja |
author_role |
author |
author2 |
Rodrigues, Luisa Cunha, Filipa M. Matos, Daniela Hildebrandt, Peter Murgida, Daniel Horacio Pereira, Inês A. C. Todorovic, Smilja |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Nitrite Reductase Raman |
topic |
Nitrite Reductase Raman |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society. Fil: Martins, Gabriel. Universidade Nova de Lisboa; Portugal Fil: Rodrigues, Luisa. Universidade Nova de Lisboa; Portugal. Instituto Gulbenkian de Ciencia; Portugal Fil: Cunha, Filipa M.. Universidade Nova de Lisboa; Portugal Fil: Matos, Daniela. Universidade Nova de Lisboa; Portugal Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina Fil: Pereira, Inês A. C.. Universidade Nova de Lisboa; Portugal Fil: Todorovic, Smilja. Universidade Nova de Lisboa; Portugal |
description |
The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-04 |
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/11336/71945 Martins, Gabriel; Rodrigues, Luisa; Cunha, Filipa M.; Matos, Daniela; Hildebrandt, Peter; et al.; Substrate binding to a nitrite reductase induces a spin transition; American Chemical Society; Journal of Physical Chemistry B; 114; 16; 4-2010; 5563-5566 1520-6106 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/71945 |
identifier_str_mv |
Martins, Gabriel; Rodrigues, Luisa; Cunha, Filipa M.; Matos, Daniela; Hildebrandt, Peter; et al.; Substrate binding to a nitrite reductase induces a spin transition; American Chemical Society; Journal of Physical Chemistry B; 114; 16; 4-2010; 5563-5566 1520-6106 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://pubs.acs.org/doi/10.1021/jp9118502 info:eu-repo/semantics/altIdentifier/doi/10.1021/jp9118502 |
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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1842268801899429888 |
score |
13.13397 |