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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/71945
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-09-29T09:37:50Zoai: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:34982025-09-29 09:37:50.557CONICET 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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score 13.070432

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