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Title: Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions
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
Keywords: Peixos
Cinètica enzimàtica
Biologia molecular
Enzyme kinetics
Molecular biology
Issue Date: 12-Aug-2020
Publisher: Research Network of Computational and Structural Biotechnology (RNCSB)
Abstract: 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.
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It is part of: Computational and Structural Biotechnology Journal, 2020, vol. 18, p. 2132-2144
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ISSN: 2001-0370
Appears in Collections:Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia)

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