Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms
- Autores
- Correa Aragunde, Maria Natalia; Foresi, Noelia Pamela; Lamattina, Lorenzo
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Humans have enormously increased the level of nitrogen (N) circulating in the troposphere and the earth surface during the last century, correlating with the population increase. As an undesirable consequence, high levels of reactive N are polluting the environment where humans inhabit. Nitric oxide (NO) is one of the reactive N species with both positive and negative impact on life. NO synthases (NOS) are enzymes that oxidize arginine to citrulline and generate the denitrifying intermediate NO which can be subsequently reduced to N2O and N2. NOS are large modular enzymes present in all kingdoms which through evolution were the result of multiple gene and genome duplication events together with changes in protein architecture (Andreakis et al. 2011). A recently described NOS from the marine unicellular microalgae Ostreococcus tauri, belonging to the picoplankton in oceans, adds new insights to study the evolution of the complex organization of these enzymes. In this opinion we discuss the structure diversity of the emerging new NOS forms described in prokaryotes and eukaryotes. Regarding the controversy about the existence of canonical NOS in higher plants, we propose that the latest findings support the existence of a high diversity of NOS forms in different lineages. Thereby, since higher plant species whose genomes have been fully sequenced, which are scarce, it cannot be discarded that a new form of NOS may have evolved in higher plants.
Fil: Correa Aragunde, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Foresi, Noelia Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina - Materia
-
nitric oxide synthase
photosynthetic microorganism
ostreococcus - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/13197
Ver los metadatos del registro completo
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Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organismsCorrea Aragunde, Maria NataliaForesi, Noelia PamelaLamattina, Lorenzonitric oxide synthasephotosynthetic microorganismostreococcushttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Humans have enormously increased the level of nitrogen (N) circulating in the troposphere and the earth surface during the last century, correlating with the population increase. As an undesirable consequence, high levels of reactive N are polluting the environment where humans inhabit. Nitric oxide (NO) is one of the reactive N species with both positive and negative impact on life. NO synthases (NOS) are enzymes that oxidize arginine to citrulline and generate the denitrifying intermediate NO which can be subsequently reduced to N2O and N2. NOS are large modular enzymes present in all kingdoms which through evolution were the result of multiple gene and genome duplication events together with changes in protein architecture (Andreakis et al. 2011). A recently described NOS from the marine unicellular microalgae Ostreococcus tauri, belonging to the picoplankton in oceans, adds new insights to study the evolution of the complex organization of these enzymes. In this opinion we discuss the structure diversity of the emerging new NOS forms described in prokaryotes and eukaryotes. Regarding the controversy about the existence of canonical NOS in higher plants, we propose that the latest findings support the existence of a high diversity of NOS forms in different lineages. Thereby, since higher plant species whose genomes have been fully sequenced, which are scarce, it cannot be discarded that a new form of NOS may have evolved in higher plants.Fil: Correa Aragunde, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Foresi, Noelia Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaUniversity of Arizona2013-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13197Correa Aragunde, Maria Natalia; Foresi, Noelia Pamela; Lamattina, Lorenzo; Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms; University of Arizona; Frontiers in Plant Science; 4; 7-2013; 232-2351664-462Xenginfo:eu-repo/semantics/altIdentifier/url/http://journal.frontiersin.org/article/10.3389/fpls.2013.00232/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2013.00232info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:57:19Zoai:ri.conicet.gov.ar:11336/13197instacron: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 09:57:20.068CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
title |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
spellingShingle |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms Correa Aragunde, Maria Natalia nitric oxide synthase photosynthetic microorganism ostreococcus |
title_short |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
title_full |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
title_fullStr |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
title_full_unstemmed |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
title_sort |
Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms |
dc.creator.none.fl_str_mv |
Correa Aragunde, Maria Natalia Foresi, Noelia Pamela Lamattina, Lorenzo |
author |
Correa Aragunde, Maria Natalia |
author_facet |
Correa Aragunde, Maria Natalia Foresi, Noelia Pamela Lamattina, Lorenzo |
author_role |
author |
author2 |
Foresi, Noelia Pamela Lamattina, Lorenzo |
author2_role |
author author |
dc.subject.none.fl_str_mv |
nitric oxide synthase photosynthetic microorganism ostreococcus |
topic |
nitric oxide synthase photosynthetic microorganism ostreococcus |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Humans have enormously increased the level of nitrogen (N) circulating in the troposphere and the earth surface during the last century, correlating with the population increase. As an undesirable consequence, high levels of reactive N are polluting the environment where humans inhabit. Nitric oxide (NO) is one of the reactive N species with both positive and negative impact on life. NO synthases (NOS) are enzymes that oxidize arginine to citrulline and generate the denitrifying intermediate NO which can be subsequently reduced to N2O and N2. NOS are large modular enzymes present in all kingdoms which through evolution were the result of multiple gene and genome duplication events together with changes in protein architecture (Andreakis et al. 2011). A recently described NOS from the marine unicellular microalgae Ostreococcus tauri, belonging to the picoplankton in oceans, adds new insights to study the evolution of the complex organization of these enzymes. In this opinion we discuss the structure diversity of the emerging new NOS forms described in prokaryotes and eukaryotes. Regarding the controversy about the existence of canonical NOS in higher plants, we propose that the latest findings support the existence of a high diversity of NOS forms in different lineages. Thereby, since higher plant species whose genomes have been fully sequenced, which are scarce, it cannot be discarded that a new form of NOS may have evolved in higher plants. Fil: Correa Aragunde, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina Fil: Foresi, Noelia Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina Fil: Lamattina, Lorenzo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina |
description |
Humans have enormously increased the level of nitrogen (N) circulating in the troposphere and the earth surface during the last century, correlating with the population increase. As an undesirable consequence, high levels of reactive N are polluting the environment where humans inhabit. Nitric oxide (NO) is one of the reactive N species with both positive and negative impact on life. NO synthases (NOS) are enzymes that oxidize arginine to citrulline and generate the denitrifying intermediate NO which can be subsequently reduced to N2O and N2. NOS are large modular enzymes present in all kingdoms which through evolution were the result of multiple gene and genome duplication events together with changes in protein architecture (Andreakis et al. 2011). A recently described NOS from the marine unicellular microalgae Ostreococcus tauri, belonging to the picoplankton in oceans, adds new insights to study the evolution of the complex organization of these enzymes. In this opinion we discuss the structure diversity of the emerging new NOS forms described in prokaryotes and eukaryotes. Regarding the controversy about the existence of canonical NOS in higher plants, we propose that the latest findings support the existence of a high diversity of NOS forms in different lineages. Thereby, since higher plant species whose genomes have been fully sequenced, which are scarce, it cannot be discarded that a new form of NOS may have evolved in higher plants. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-07 |
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/11336/13197 Correa Aragunde, Maria Natalia; Foresi, Noelia Pamela; Lamattina, Lorenzo; Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms; University of Arizona; Frontiers in Plant Science; 4; 7-2013; 232-235 1664-462X |
url |
http://hdl.handle.net/11336/13197 |
identifier_str_mv |
Correa Aragunde, Maria Natalia; Foresi, Noelia Pamela; Lamattina, Lorenzo; Structure diversity of nitric oxide synthases (NOS): the emergence of new forms in photosynthetic organisms; University of Arizona; Frontiers in Plant Science; 4; 7-2013; 232-235 1664-462X |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://journal.frontiersin.org/article/10.3389/fpls.2013.00232/full info:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2013.00232 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
University of Arizona |
publisher.none.fl_str_mv |
University of Arizona |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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