The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics

Autores
Giordano, Daniela; Boechi, Leonardo; Vergara, Alessandro; Marti, Marcelo Adrian; Samuni, Uri; Dantsker, David; Grassi, Luigi; Estrin, Dario Ariel; Friedman, Joel M.; Mazzarella, Lelio; Di Prisco, Guido; Verde, Cinzia
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The dominant perciform suborder Notothenioidei is an excellent study group for assessing the evolution and functional importance of biochemical adaptations to temperature. The availability of notothenioid taxa in a wide range of latitudes (Antarctic and non-Antarctic) provides a tool to enable identification of physiological and biochemical characteristics gained and lost during evolutionary history. Non-Antarctic notothenioids belonging to the most basal families are a crucial source for understanding the evolution of hemoglobin in high-Antarctic cold-adapted fish. This paper focuses on the structure, function and evolution of the oxygen-transport system of Cottoperca gobio, a sub-Antarctic notothenioid fish of the family Bovichtidae, probably derived from ancestral species that evolved in the Antarctic region and later migrated to lower latitudes. Unlike most high-Antarctic notothenioids, but similar to many other acanthomorph teleosts, C. gobio has two major hemoglobins having the β chain in common. The oxygen-binding equilibria and kinetics of the two hemoglobins have been measured. Hb1 and Hb2 show strong modulation of oxygen-binding equilibria and kinetics by heterotropic effectors, with marked Bohr and Root effects. In Hb1 and Hb2, oxygen affinity and subunit cooperativity are slightly higher than in most high-Antarctic notothenioid hemoglobins. Hb1 and Hb2 show similar rebinding rates, but also show significant dynamic differences that are likely to have functional consequences. Molecular dynamic simulations of C. gobio Hb1 were performed on the dimeric protein in order to obtain a better understanding of the molecular basis of structure/function relationships.
Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; Italia
Fil: Boechi, Leonardo. 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: Vergara, Alessandro. Università degli Studi di Napoli Federico II; Italia
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: Samuni, Uri. City University of New York; Estados Unidos
Fil: Dantsker, David. Albert Einstein College of Medicine; Estados Unidos
Fil: Grassi, Luigi. Consiglio Nazionale delle Ricerche; Italia
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: Friedman, Joel M.. Albert Einstein College of Medicine; Estados Unidos
Fil: Mazzarella, Lelio. Università degli Studi di Napoli Federico II; Italia
Fil: Di Prisco, Guido. Consiglio Nazionale delle Ricerche; Italia
Fil: Verde, Cinzia. Consiglio Nazionale delle Ricerche; Italia
Materia
Antarctica
Computer Simulation
Hemoglobin
Ligand-Binding Properties
Oxygen Affinity
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:11336/74803
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/74803
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamicsGiordano, DanielaBoechi, LeonardoVergara, AlessandroMarti, Marcelo AdrianSamuni, UriDantsker, DavidGrassi, LuigiEstrin, Dario ArielFriedman, Joel M.Mazzarella, LelioDi Prisco, GuidoVerde, CinziaAntarcticaComputer SimulationHemoglobinLigand-Binding PropertiesOxygen Affinityhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The dominant perciform suborder Notothenioidei is an excellent study group for assessing the evolution and functional importance of biochemical adaptations to temperature. The availability of notothenioid taxa in a wide range of latitudes (Antarctic and non-Antarctic) provides a tool to enable identification of physiological and biochemical characteristics gained and lost during evolutionary history. Non-Antarctic notothenioids belonging to the most basal families are a crucial source for understanding the evolution of hemoglobin in high-Antarctic cold-adapted fish. This paper focuses on the structure, function and evolution of the oxygen-transport system of Cottoperca gobio, a sub-Antarctic notothenioid fish of the family Bovichtidae, probably derived from ancestral species that evolved in the Antarctic region and later migrated to lower latitudes. Unlike most high-Antarctic notothenioids, but similar to many other acanthomorph teleosts, C. gobio has two major hemoglobins having the β chain in common. The oxygen-binding equilibria and kinetics of the two hemoglobins have been measured. Hb1 and Hb2 show strong modulation of oxygen-binding equilibria and kinetics by heterotropic effectors, with marked Bohr and Root effects. In Hb1 and Hb2, oxygen affinity and subunit cooperativity are slightly higher than in most high-Antarctic notothenioid hemoglobins. Hb1 and Hb2 show similar rebinding rates, but also show significant dynamic differences that are likely to have functional consequences. Molecular dynamic simulations of C. gobio Hb1 were performed on the dimeric protein in order to obtain a better understanding of the molecular basis of structure/function relationships.Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; ItaliaFil: Boechi, Leonardo. 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: Vergara, Alessandro. Università degli Studi di Napoli Federico II; ItaliaFil: 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: Samuni, Uri. City University of New York; Estados UnidosFil: Dantsker, David. Albert Einstein College of Medicine; Estados UnidosFil: Grassi, Luigi. Consiglio Nazionale delle Ricerche; ItaliaFil: 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: Friedman, Joel M.. Albert Einstein College of Medicine; Estados UnidosFil: Mazzarella, Lelio. Università degli Studi di Napoli Federico II; ItaliaFil: Di Prisco, Guido. Consiglio Nazionale delle Ricerche; ItaliaFil: Verde, Cinzia. Consiglio Nazionale delle Ricerche; ItaliaWiley Blackwell Publishing, Inc2009-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/74803Giordano, Daniela; Boechi, Leonardo; Vergara, Alessandro; Marti, Marcelo Adrian; Samuni, Uri; et al.; The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics; Wiley Blackwell Publishing, Inc; Febs Journal; 276; 8; 4-2009; 2266-22771742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2009.06954.xinfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2009.06954.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:19Zoai:ri.conicet.gov.ar:11336/74803instacron: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 09:36:20.168CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
title The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
spellingShingle The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
Giordano, Daniela
Antarctica
Computer Simulation
Hemoglobin
Ligand-Binding Properties
Oxygen Affinity
title_short The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
title_full The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
title_fullStr The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
title_full_unstemmed The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
title_sort The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics
dc.creator.none.fl_str_mv Giordano, Daniela
Boechi, Leonardo
Vergara, Alessandro
Marti, Marcelo Adrian
Samuni, Uri
Dantsker, David
Grassi, Luigi
Estrin, Dario Ariel
Friedman, Joel M.
Mazzarella, Lelio
Di Prisco, Guido
Verde, Cinzia
author Giordano, Daniela
author_facet Giordano, Daniela
Boechi, Leonardo
Vergara, Alessandro
Marti, Marcelo Adrian
Samuni, Uri
Dantsker, David
Grassi, Luigi
Estrin, Dario Ariel
Friedman, Joel M.
Mazzarella, Lelio
Di Prisco, Guido
Verde, Cinzia
author_role author
author2 Boechi, Leonardo
Vergara, Alessandro
Marti, Marcelo Adrian
Samuni, Uri
Dantsker, David
Grassi, Luigi
Estrin, Dario Ariel
Friedman, Joel M.
Mazzarella, Lelio
Di Prisco, Guido
Verde, Cinzia
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Antarctica
Computer Simulation
Hemoglobin
Ligand-Binding Properties
Oxygen Affinity
topic Antarctica
Computer Simulation
Hemoglobin
Ligand-Binding Properties
Oxygen Affinity
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 dominant perciform suborder Notothenioidei is an excellent study group for assessing the evolution and functional importance of biochemical adaptations to temperature. The availability of notothenioid taxa in a wide range of latitudes (Antarctic and non-Antarctic) provides a tool to enable identification of physiological and biochemical characteristics gained and lost during evolutionary history. Non-Antarctic notothenioids belonging to the most basal families are a crucial source for understanding the evolution of hemoglobin in high-Antarctic cold-adapted fish. This paper focuses on the structure, function and evolution of the oxygen-transport system of Cottoperca gobio, a sub-Antarctic notothenioid fish of the family Bovichtidae, probably derived from ancestral species that evolved in the Antarctic region and later migrated to lower latitudes. Unlike most high-Antarctic notothenioids, but similar to many other acanthomorph teleosts, C. gobio has two major hemoglobins having the β chain in common. The oxygen-binding equilibria and kinetics of the two hemoglobins have been measured. Hb1 and Hb2 show strong modulation of oxygen-binding equilibria and kinetics by heterotropic effectors, with marked Bohr and Root effects. In Hb1 and Hb2, oxygen affinity and subunit cooperativity are slightly higher than in most high-Antarctic notothenioid hemoglobins. Hb1 and Hb2 show similar rebinding rates, but also show significant dynamic differences that are likely to have functional consequences. Molecular dynamic simulations of C. gobio Hb1 were performed on the dimeric protein in order to obtain a better understanding of the molecular basis of structure/function relationships.
Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; Italia
Fil: Boechi, Leonardo. 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: Vergara, Alessandro. Università degli Studi di Napoli Federico II; Italia
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: Samuni, Uri. City University of New York; Estados Unidos
Fil: Dantsker, David. Albert Einstein College of Medicine; Estados Unidos
Fil: Grassi, Luigi. Consiglio Nazionale delle Ricerche; Italia
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: Friedman, Joel M.. Albert Einstein College of Medicine; Estados Unidos
Fil: Mazzarella, Lelio. Università degli Studi di Napoli Federico II; Italia
Fil: Di Prisco, Guido. Consiglio Nazionale delle Ricerche; Italia
Fil: Verde, Cinzia. Consiglio Nazionale delle Ricerche; Italia
description The dominant perciform suborder Notothenioidei is an excellent study group for assessing the evolution and functional importance of biochemical adaptations to temperature. The availability of notothenioid taxa in a wide range of latitudes (Antarctic and non-Antarctic) provides a tool to enable identification of physiological and biochemical characteristics gained and lost during evolutionary history. Non-Antarctic notothenioids belonging to the most basal families are a crucial source for understanding the evolution of hemoglobin in high-Antarctic cold-adapted fish. This paper focuses on the structure, function and evolution of the oxygen-transport system of Cottoperca gobio, a sub-Antarctic notothenioid fish of the family Bovichtidae, probably derived from ancestral species that evolved in the Antarctic region and later migrated to lower latitudes. Unlike most high-Antarctic notothenioids, but similar to many other acanthomorph teleosts, C. gobio has two major hemoglobins having the β chain in common. The oxygen-binding equilibria and kinetics of the two hemoglobins have been measured. Hb1 and Hb2 show strong modulation of oxygen-binding equilibria and kinetics by heterotropic effectors, with marked Bohr and Root effects. In Hb1 and Hb2, oxygen affinity and subunit cooperativity are slightly higher than in most high-Antarctic notothenioid hemoglobins. Hb1 and Hb2 show similar rebinding rates, but also show significant dynamic differences that are likely to have functional consequences. Molecular dynamic simulations of C. gobio Hb1 were performed on the dimeric protein in order to obtain a better understanding of the molecular basis of structure/function relationships.
publishDate 2009
dc.date.none.fl_str_mv 2009-04
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/11336/74803
Giordano, Daniela; Boechi, Leonardo; Vergara, Alessandro; Marti, Marcelo Adrian; Samuni, Uri; et al.; The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics; Wiley Blackwell Publishing, Inc; Febs Journal; 276; 8; 4-2009; 2266-2277
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/74803
identifier_str_mv Giordano, Daniela; Boechi, Leonardo; Vergara, Alessandro; Marti, Marcelo Adrian; Samuni, Uri; et al.; The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics; Wiley Blackwell Publishing, Inc; Febs Journal; 276; 8; 4-2009; 2266-2277
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2009.06954.x
info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2009.06954.x
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
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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