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

Daniela Giordano, Leonardo Boechi, Alessandro Vergara, Marcelo A. Martí, Uri Samuni, David Dantsker, Luigi Grassi, Darío A. Estrin, Joel M. Friedman, Lelio Mazzarella, Guido Di Prisco, Cinzia Verde

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2266-2277
Number of pages12
JournalFEBS Journal
Volume276
Issue number8
DOIs
StatePublished - Apr 2009

Fingerprint

Molecular Dynamics Simulation
Fish
Molecular dynamics
Fishes
Hemoglobins
Oxygen
Kinetics
Antarctic Regions
Molecular Structure
History
Modulation
Availability
Temperature
Computer simulation
Proteins

Keywords

  • Antarctica
  • Computer simulation
  • Hemoglobin
  • Ligand-binding properties
  • Oxygen affinity

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics. / Giordano, Daniela; Boechi, Leonardo; Vergara, Alessandro; Martí, Marcelo A.; Samuni, Uri; Dantsker, David; Grassi, Luigi; Estrin, Darío A.; Friedman, Joel M.; Mazzarella, Lelio; Di Prisco, Guido; Verde, Cinzia.

In: FEBS Journal, Vol. 276, No. 8, 04.2009, p. 2266-2277.

Research output: Contribution to journalArticle

Giordano, D, Boechi, L, Vergara, A, Martí, MA, Samuni, U, Dantsker, D, Grassi, L, Estrin, DA, Friedman, JM, Mazzarella, L, Di Prisco, G & Verde, C 2009, 'The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics', FEBS Journal, vol. 276, no. 8, pp. 2266-2277. https://doi.org/10.1111/j.1742-4658.2009.06954.x
Giordano, Daniela ; Boechi, Leonardo ; Vergara, Alessandro ; Martí, Marcelo A. ; Samuni, Uri ; Dantsker, David ; Grassi, Luigi ; Estrin, Darío A. ; Friedman, Joel M. ; Mazzarella, Lelio ; Di Prisco, Guido ; Verde, Cinzia. / The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species - Oxygen-binding equilibria, kinetics and molecular dynamics. In: FEBS Journal. 2009 ; Vol. 276, No. 8. pp. 2266-2277.
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abstract = "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.",
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