Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling
- Autores
- Singh, Sandeep; Thakur, Naveen; Oliveira, Ana; Petruk, Ariel Alcides; Hade, Mangesh Dattu; Sethi, Deepti; Bidon Chanal, Axel; Marti, Marcelo Adrian; Datta, H.; Parkesh, R.; Estrin, Dario Ariel; Luque, F. Javier; Dikshit, Kanak L.
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are modulated by its CD loop and the Pre-A region. Significance: The present study provides new insights into the mechanism of electron transfer during nitric oxide detoxification by HbN.
Fil: Singh, Sandeep. Institute of Microbial Technology; India
Fil: Thakur, Naveen. Institute of Microbial Technology; India
Fil: Oliveira, Ana. Universidad de Barcelona; España
Fil: Petruk, Ariel Alcides. 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
Fil: Hade, Mangesh Dattu. Institute of Microbial Technology; India
Fil: Sethi, Deepti. Institute of Microbial Technology; India
Fil: Bidon Chanal, Axel. Universidad de Barcelona; España
Fil: Marti, Marcelo Adrian. 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
Fil: Datta, H.. Institute of Microbial Technology; India
Fil: Parkesh, R.. Institute of Microbial Technology; India
Fil: Estrin, Dario Ariel. 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
Fil: Luque, F. Javier. Universidad de Barcelona; España
Fil: Dikshit, Kanak L.. Institute of Microbial Technology; India - Materia
-
Truncated hemoglobin
Tuberculosis
Electron transfer - 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:11336/31877
Ver los metadatos del registro completo
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Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cyclingSingh, SandeepThakur, NaveenOliveira, AnaPetruk, Ariel AlcidesHade, Mangesh DattuSethi, DeeptiBidon Chanal, AxelMarti, Marcelo AdrianDatta, H.Parkesh, R.Estrin, Dario ArielLuque, F. JavierDikshit, Kanak L.Truncated hemoglobinTuberculosisElectron transferhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are modulated by its CD loop and the Pre-A region. Significance: The present study provides new insights into the mechanism of electron transfer during nitric oxide detoxification by HbN.Fil: Singh, Sandeep. Institute of Microbial Technology; IndiaFil: Thakur, Naveen. Institute of Microbial Technology; IndiaFil: Oliveira, Ana. Universidad de Barcelona; EspañaFil: Petruk, Ariel Alcides. 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; ArgentinaFil: Hade, Mangesh Dattu. Institute of Microbial Technology; IndiaFil: Sethi, Deepti. Institute of Microbial Technology; IndiaFil: Bidon Chanal, Axel. Universidad de Barcelona; EspañaFil: Marti, Marcelo Adrian. 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; ArgentinaFil: Datta, H.. Institute of Microbial Technology; IndiaFil: Parkesh, R.. Institute of Microbial Technology; IndiaFil: Estrin, Dario Ariel. 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; ArgentinaFil: Luque, F. Javier. Universidad de Barcelona; EspañaFil: Dikshit, Kanak L.. Institute of Microbial Technology; IndiaAmerican Society for Biochemistry and Molecular Biology2014-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31877Dikshit, Kanak L.; Luque, F. Javier; Estrin, Dario Ariel; Parkesh, R.; Datta, H.; Marti, Marcelo Adrian; et al.; Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling ; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 6-2014; 21573-215830021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M114.578187info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/289/31/21573info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:57Zoai:ri.conicet.gov.ar:11336/31877instacron: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 09:36:57.562CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
title |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
spellingShingle |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling Singh, Sandeep Truncated hemoglobin Tuberculosis Electron transfer |
title_short |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
title_full |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
title_fullStr |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
title_full_unstemmed |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
title_sort |
Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling |
dc.creator.none.fl_str_mv |
Singh, Sandeep Thakur, Naveen Oliveira, Ana Petruk, Ariel Alcides Hade, Mangesh Dattu Sethi, Deepti Bidon Chanal, Axel Marti, Marcelo Adrian Datta, H. Parkesh, R. Estrin, Dario Ariel Luque, F. Javier Dikshit, Kanak L. |
author |
Singh, Sandeep |
author_facet |
Singh, Sandeep Thakur, Naveen Oliveira, Ana Petruk, Ariel Alcides Hade, Mangesh Dattu Sethi, Deepti Bidon Chanal, Axel Marti, Marcelo Adrian Datta, H. Parkesh, R. Estrin, Dario Ariel Luque, F. Javier Dikshit, Kanak L. |
author_role |
author |
author2 |
Thakur, Naveen Oliveira, Ana Petruk, Ariel Alcides Hade, Mangesh Dattu Sethi, Deepti Bidon Chanal, Axel Marti, Marcelo Adrian Datta, H. Parkesh, R. Estrin, Dario Ariel Luque, F. Javier Dikshit, Kanak L. |
author2_role |
author author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Truncated hemoglobin Tuberculosis Electron transfer |
topic |
Truncated hemoglobin Tuberculosis Electron transfer |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are modulated by its CD loop and the Pre-A region. Significance: The present study provides new insights into the mechanism of electron transfer during nitric oxide detoxification by HbN. Fil: Singh, Sandeep. Institute of Microbial Technology; India Fil: Thakur, Naveen. Institute of Microbial Technology; India Fil: Oliveira, Ana. Universidad de Barcelona; España Fil: Petruk, Ariel Alcides. 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 Fil: Hade, Mangesh Dattu. Institute of Microbial Technology; India Fil: Sethi, Deepti. Institute of Microbial Technology; India Fil: Bidon Chanal, Axel. Universidad de Barcelona; España Fil: Marti, Marcelo Adrian. 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 Fil: Datta, H.. Institute of Microbial Technology; India Fil: Parkesh, R.. Institute of Microbial Technology; India Fil: Estrin, Dario Ariel. 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 Fil: Luque, F. Javier. Universidad de Barcelona; España Fil: Dikshit, Kanak L.. Institute of Microbial Technology; India |
description |
Background: The HbN of Mycobacterium tuberculosis carries a potent nitric-oxide dioxygenase activity despite lacking a reductase domain. Results: The NADH-ferredoxin reductase system acts as an efficient partner for the reduction of HbN. Conclusion: The interactions of HbN with the reductase are modulated by its CD loop and the Pre-A region. Significance: The present study provides new insights into the mechanism of electron transfer during nitric oxide detoxification by HbN. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-06 |
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/11336/31877 Dikshit, Kanak L.; Luque, F. Javier; Estrin, Dario Ariel; Parkesh, R.; Datta, H.; Marti, Marcelo Adrian; et al.; Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling ; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 6-2014; 21573-21583 0021-9258 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/31877 |
identifier_str_mv |
Dikshit, Kanak L.; Luque, F. Javier; Estrin, Dario Ariel; Parkesh, R.; Datta, H.; Marti, Marcelo Adrian; et al.; Mechanistic Insight into the Enzymatic Reduction of Truncated Hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A Motif in electron cycling ; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 289; 6-2014; 21573-21583 0021-9258 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M114.578187 info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/289/31/21573 |
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 Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
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) |
collection |
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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1844613162678091776 |
score |
13.070432 |