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Artículo

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

Giordano, Daniela; Boechi, LeonardoIcon ; Vergara, Alessandro; Marti, Marcelo AdrianIcon ; Samuni, Uri; Dantsker, David; Grassi, Luigi; Estrin, Dario ArielIcon ; Friedman, Joel M.; Mazzarella, Lelio; Di Prisco, Guido; Verde, Cinzia
Fecha de publicación: 04/2009
Editorial: Wiley Blackwell Publishing, Inc
Revista: Febs Journal
ISSN: 1742-464X
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Otras Ciencias Químicas

Resumen

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.
Palabras clave: Antarctica , Computer Simulation , Hemoglobin , Ligand-Binding Properties , Oxygen Affinity
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/74803
DOI: http://dx.doi.org/10.1111/j.1742-4658.2009.06954.x
URL: https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2009.06954.x
Colecciones
Articulos(INQUIMAE)
Articulos de INST.D/QUIM FIS D/L MATERIALES MEDIOAMB Y ENERGIA
Citación
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
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