Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor
- Autores
- Hernandez, Jose A.; Curatti, Leonardo; Aznar, Constantino P.; Perova, Zinaida; Britt, R. David; Rubio, Luis M.
- Año de publicación
- 2008
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The molybdenum nitrogenase, present in a diverse group of bacteria and archea, is the major contributor to biological nitrogen fixation. The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo, one unidentified light atom, and homocitrate. The nifQ gene was known to be involved in the incorporation of molybdenum into nitrogenase. Here we show direct biochemical evidence for the role of NifQ in FeMo-co biosynthesis. As-isolated NifQ was found to carry a molybdenum-iron-sulfur cluster that serves as a specific molybdenum donor for FeMo-co biosynthesis. Purified NifQ supported in vitro FeMo-co synthesis in the absence of an additional molybdenum source. The mobilization of molybdenum from NifQ required the simultaneous participation of NifH and NifEN in the in vitro FeMo-co synthesis assay, suggesting that NifQ would be the physiological molybdenum donor to a hypothetical NifEN/NifH complex.
Fil: Hernandez, Jose A.. University of California; Estados Unidos
Fil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina
Fil: Aznar, Constantino P.. University of California; Estados Unidos
Fil: Perova, Zinaida. University of California; Estados Unidos
Fil: Britt, R. David. University of California; Estados Unidos
Fil: Rubio, Luis M.. University of California; Estados Unidos - Materia
-
AZOTOBACTER VINELANDII
IRON-SULFUR CLUSTER
NIF - 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:11336/132499
Ver los metadatos del registro completo
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Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactorHernandez, Jose A.Curatti, LeonardoAznar, Constantino P.Perova, ZinaidaBritt, R. DavidRubio, Luis M.AZOTOBACTER VINELANDIIIRON-SULFUR CLUSTERNIFhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The molybdenum nitrogenase, present in a diverse group of bacteria and archea, is the major contributor to biological nitrogen fixation. The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo, one unidentified light atom, and homocitrate. The nifQ gene was known to be involved in the incorporation of molybdenum into nitrogenase. Here we show direct biochemical evidence for the role of NifQ in FeMo-co biosynthesis. As-isolated NifQ was found to carry a molybdenum-iron-sulfur cluster that serves as a specific molybdenum donor for FeMo-co biosynthesis. Purified NifQ supported in vitro FeMo-co synthesis in the absence of an additional molybdenum source. The mobilization of molybdenum from NifQ required the simultaneous participation of NifH and NifEN in the in vitro FeMo-co synthesis assay, suggesting that NifQ would be the physiological molybdenum donor to a hypothetical NifEN/NifH complex.Fil: Hernandez, Jose A.. University of California; Estados UnidosFil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; ArgentinaFil: Aznar, Constantino P.. University of California; Estados UnidosFil: Perova, Zinaida. University of California; Estados UnidosFil: Britt, R. David. University of California; Estados UnidosFil: Rubio, Luis M.. University of California; Estados UnidosNational Academy of Sciences2008-08-19info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/132499Hernandez, Jose A.; Curatti, Leonardo; Aznar, Constantino P.; Perova, Zinaida; Britt, R. David; et al.; Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 105; 33; 19-8-2008; 11679-116840027-84241091-6490CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0803576105info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/105/33/11679info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:39:59Zoai:ri.conicet.gov.ar:11336/132499instacron: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 10:39:59.622CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
title |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
spellingShingle |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor Hernandez, Jose A. AZOTOBACTER VINELANDII IRON-SULFUR CLUSTER NIF |
title_short |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
title_full |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
title_fullStr |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
title_full_unstemmed |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
title_sort |
Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor |
dc.creator.none.fl_str_mv |
Hernandez, Jose A. Curatti, Leonardo Aznar, Constantino P. Perova, Zinaida Britt, R. David Rubio, Luis M. |
author |
Hernandez, Jose A. |
author_facet |
Hernandez, Jose A. Curatti, Leonardo Aznar, Constantino P. Perova, Zinaida Britt, R. David Rubio, Luis M. |
author_role |
author |
author2 |
Curatti, Leonardo Aznar, Constantino P. Perova, Zinaida Britt, R. David Rubio, Luis M. |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
AZOTOBACTER VINELANDII IRON-SULFUR CLUSTER NIF |
topic |
AZOTOBACTER VINELANDII IRON-SULFUR CLUSTER NIF |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The molybdenum nitrogenase, present in a diverse group of bacteria and archea, is the major contributor to biological nitrogen fixation. The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo, one unidentified light atom, and homocitrate. The nifQ gene was known to be involved in the incorporation of molybdenum into nitrogenase. Here we show direct biochemical evidence for the role of NifQ in FeMo-co biosynthesis. As-isolated NifQ was found to carry a molybdenum-iron-sulfur cluster that serves as a specific molybdenum donor for FeMo-co biosynthesis. Purified NifQ supported in vitro FeMo-co synthesis in the absence of an additional molybdenum source. The mobilization of molybdenum from NifQ required the simultaneous participation of NifH and NifEN in the in vitro FeMo-co synthesis assay, suggesting that NifQ would be the physiological molybdenum donor to a hypothetical NifEN/NifH complex. Fil: Hernandez, Jose A.. University of California; Estados Unidos Fil: Curatti, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario; Argentina Fil: Aznar, Constantino P.. University of California; Estados Unidos Fil: Perova, Zinaida. University of California; Estados Unidos Fil: Britt, R. David. University of California; Estados Unidos Fil: Rubio, Luis M.. University of California; Estados Unidos |
description |
The molybdenum nitrogenase, present in a diverse group of bacteria and archea, is the major contributor to biological nitrogen fixation. The nitrogenase active site contains an iron-molybdenum cofactor (FeMo-co) composed of 7Fe, 9S, 1Mo, one unidentified light atom, and homocitrate. The nifQ gene was known to be involved in the incorporation of molybdenum into nitrogenase. Here we show direct biochemical evidence for the role of NifQ in FeMo-co biosynthesis. As-isolated NifQ was found to carry a molybdenum-iron-sulfur cluster that serves as a specific molybdenum donor for FeMo-co biosynthesis. Purified NifQ supported in vitro FeMo-co synthesis in the absence of an additional molybdenum source. The mobilization of molybdenum from NifQ required the simultaneous participation of NifH and NifEN in the in vitro FeMo-co synthesis assay, suggesting that NifQ would be the physiological molybdenum donor to a hypothetical NifEN/NifH complex. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-08-19 |
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/11336/132499 Hernandez, Jose A.; Curatti, Leonardo; Aznar, Constantino P.; Perova, Zinaida; Britt, R. David; et al.; Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 105; 33; 19-8-2008; 11679-11684 0027-8424 1091-6490 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/132499 |
identifier_str_mv |
Hernandez, Jose A.; Curatti, Leonardo; Aznar, Constantino P.; Perova, Zinaida; Britt, R. David; et al.; Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 105; 33; 19-8-2008; 11679-11684 0027-8424 1091-6490 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0803576105 info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/105/33/11679 |
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 |
National Academy of Sciences |
publisher.none.fl_str_mv |
National Academy of Sciences |
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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1844614426583367680 |
score |
13.070432 |