Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions
While the functions of the recently discovered cytoglobin, ubiquitously expressed in vertebrate tissues, remain uncertain, Antarctic fish provide unparalleled models to study novel protein traits that may arise from cold adaptation. We report here the spectral, ligand-binding and enzymatic propertie...
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ftubarcepubl:oai:diposit.ub.edu:2445/174435 2024-02-11T09:56:38+01:00 Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions Giordano, Daniela Pesce, Alessandra Vermeylen, Stijn Abbruzzetti, Stefania Nardini, Marco Marchesani, Francesco Berghmans, Herald Seira Castán, Constantí Bruno, Stefano Luque Garriga, F. Xavier di Prisco, Guido Ascenzii, Paolo Dewilde, Sylvia Bolognesi, Martino Viappiani, Cristiano Verde, Cinzia 2020-08-12 13 p. application/pdf http://hdl.handle.net/2445/174435 eng eng Research Network of Computational and Structural Biotechnology (RNCSB) Reproducció del document publicat a: https://doi.org/10.1016/j.csbj.2020.08.007 Computational and Structural Biotechnology Journal, 2020, vol. 18, p. 2132-2144 Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia) https://doi.org/10.1016/j.csbj.2020.08.007 2001-0370 http://hdl.handle.net/2445/174435 703141 32913582 cc-by-nc-nd (c) Giordano, Daniela et al., 2020 http://creativecommons.org/licenses/by-nc-nd/3.0/es info:eu-repo/semantics/openAccess Peixos Genètica Cinètica enzimàtica Metabolisme Biologia molecular Fishes Genetics Enzyme kinetics Metabolism Molecular biology info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2020 ftubarcepubl https://doi.org/10.1016/j.csbj.2020.08.007 2024-01-24T01:14:16Z While the functions of the recently discovered cytoglobin, ubiquitously expressed in vertebrate tissues, remain uncertain, Antarctic fish provide unparalleled models to study novel protein traits that may arise from cold adaptation. We report here the spectral, ligand-binding and enzymatic properties (peroxynitrite isomerization, nitrite-reductase activity) of cytoglobin-1 from two Antarctic fish, Chaenocephalus aceratus and Dissostichus mawsoni, and present the crystal structure of D. mawsoni cytoglobin-1. The Antarctic cytoglobins-1 display high O2 affinity, scarcely compatible with an O2-supply role, a slow rate constant for nitrite-reductase activity, and do not catalyze peroxynitrite isomerization. Compared with mesophilic orthologues, the cold-adapted cytoglobins favor binding of exogenous ligands to the hexa-coordinated bis-histidyl species, a trait related to their higher rate constant for distal-His/heme-Fe dissociation relative to human cytoglobin. At the light of a remarkable 3D-structure conservation, the observed differences in ligand-binding kinetics may reflect Antarctic fish cytoglobin-1 specific features in the dynamics of the heme distal region and of protein matrix cavities, suggesting adaptation to functional requirements posed by the cold environment. Taken together, the biochemical and biophysical data presented suggest that in Antarctic fish, as in humans, cytoglobin-1 unlikely plays a role in O2 transport, rather it may be involved in processes such as NO detoxification. Article in Journal/Newspaper Antarc* Antarctic Dipòsit Digital de la Universitat de Barcelona Antarctic The Antarctic Computational and Structural Biotechnology Journal 18 2132 2144 |
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Open Polar |
collection |
Dipòsit Digital de la Universitat de Barcelona |
op_collection_id |
ftubarcepubl |
language |
English |
topic |
Peixos Genètica Cinètica enzimàtica Metabolisme Biologia molecular Fishes Genetics Enzyme kinetics Metabolism Molecular biology |
spellingShingle |
Peixos Genètica Cinètica enzimàtica Metabolisme Biologia molecular Fishes Genetics Enzyme kinetics Metabolism Molecular biology Giordano, Daniela Pesce, Alessandra Vermeylen, Stijn Abbruzzetti, Stefania Nardini, Marco Marchesani, Francesco Berghmans, Herald Seira Castán, Constantí Bruno, Stefano Luque Garriga, F. Xavier di Prisco, Guido Ascenzii, Paolo Dewilde, Sylvia Bolognesi, Martino Viappiani, Cristiano Verde, Cinzia Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
topic_facet |
Peixos Genètica Cinètica enzimàtica Metabolisme Biologia molecular Fishes Genetics Enzyme kinetics Metabolism Molecular biology |
description |
While the functions of the recently discovered cytoglobin, ubiquitously expressed in vertebrate tissues, remain uncertain, Antarctic fish provide unparalleled models to study novel protein traits that may arise from cold adaptation. We report here the spectral, ligand-binding and enzymatic properties (peroxynitrite isomerization, nitrite-reductase activity) of cytoglobin-1 from two Antarctic fish, Chaenocephalus aceratus and Dissostichus mawsoni, and present the crystal structure of D. mawsoni cytoglobin-1. The Antarctic cytoglobins-1 display high O2 affinity, scarcely compatible with an O2-supply role, a slow rate constant for nitrite-reductase activity, and do not catalyze peroxynitrite isomerization. Compared with mesophilic orthologues, the cold-adapted cytoglobins favor binding of exogenous ligands to the hexa-coordinated bis-histidyl species, a trait related to their higher rate constant for distal-His/heme-Fe dissociation relative to human cytoglobin. At the light of a remarkable 3D-structure conservation, the observed differences in ligand-binding kinetics may reflect Antarctic fish cytoglobin-1 specific features in the dynamics of the heme distal region and of protein matrix cavities, suggesting adaptation to functional requirements posed by the cold environment. Taken together, the biochemical and biophysical data presented suggest that in Antarctic fish, as in humans, cytoglobin-1 unlikely plays a role in O2 transport, rather it may be involved in processes such as NO detoxification. |
format |
Article in Journal/Newspaper |
author |
Giordano, Daniela Pesce, Alessandra Vermeylen, Stijn Abbruzzetti, Stefania Nardini, Marco Marchesani, Francesco Berghmans, Herald Seira Castán, Constantí Bruno, Stefano Luque Garriga, F. Xavier di Prisco, Guido Ascenzii, Paolo Dewilde, Sylvia Bolognesi, Martino Viappiani, Cristiano Verde, Cinzia |
author_facet |
Giordano, Daniela Pesce, Alessandra Vermeylen, Stijn Abbruzzetti, Stefania Nardini, Marco Marchesani, Francesco Berghmans, Herald Seira Castán, Constantí Bruno, Stefano Luque Garriga, F. Xavier di Prisco, Guido Ascenzii, Paolo Dewilde, Sylvia Bolognesi, Martino Viappiani, Cristiano Verde, Cinzia |
author_sort |
Giordano, Daniela |
title |
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
title_short |
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
title_full |
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
title_fullStr |
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
title_full_unstemmed |
Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions |
title_sort |
structural and functional properties of antarctic fish cytoglobins-1: cold-reactivity in multi-ligand reactions |
publisher |
Research Network of Computational and Structural Biotechnology (RNCSB) |
publishDate |
2020 |
url |
http://hdl.handle.net/2445/174435 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
Reproducció del document publicat a: https://doi.org/10.1016/j.csbj.2020.08.007 Computational and Structural Biotechnology Journal, 2020, vol. 18, p. 2132-2144 Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia) https://doi.org/10.1016/j.csbj.2020.08.007 2001-0370 http://hdl.handle.net/2445/174435 703141 32913582 |
op_rights |
cc-by-nc-nd (c) Giordano, Daniela et al., 2020 http://creativecommons.org/licenses/by-nc-nd/3.0/es info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1016/j.csbj.2020.08.007 |
container_title |
Computational and Structural Biotechnology Journal |
container_volume |
18 |
container_start_page |
2132 |
op_container_end_page |
2144 |
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1790604671494127616 |