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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13197

id CONICETDig_9594fcccb634279a74985a009c341e29
oai_identifier_str oai:ri.conicet.gov.ar:11336/13197
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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
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
_version_ 1842269456642867200
score 13.13397