1. Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions
- Author
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Herald Berghmans, Paolo Ascenzi, Marco Nardini, Cinzia Verde, Daniela Giordano, Francesco Marchesani, Stijn Vermeylen, Stefania Abbruzzetti, Martino Bolognesi, Cristiano Viappiani, Constantí Seira, Guido di Prisco, Sylvia Dewilde, Alessandra Pesce, Stefano Bruno, and F. Javier Luque
- Subjects
Myoglobin ,NGB ,CO, Carbon monoxide ,Cytoglobin-1 of C. aceratus ,CO ,Molecular biology ,C.aceCygb-1*, Mutant of C.aceCygb-1 ,Human neuroglobin ,NO dioxygenase ,NO ,Ligand properties ,Penta-coordinated Cygb ,Cytoglobin ,D.mawCygb-1 ,Chaenocephalus aceratus ,Cytoglobin 2 ,Cygbh ,Biochemistry ,Cygb-1, Cytoglobin 1 ,Nitric oxide ,RNS ,chemistry.chemical_compound ,p50, O2 partial pressure required to achieve half saturation ,0302 clinical medicine ,Cold-adaptation ,Structural Biology ,Cinètica enzimàtica ,Heme ,NGB, Human neuroglobin ,chemistry.chemical_classification ,0303 health sciences ,Reactive Nitrogen Species ,ROS ,biology ,Chemistry ,Mutant of D.mawCygb-1 ,Reactive Oxygen Species ,X-ray structure ,p50 ,Fishes ,Human Cygb ,Cygb ,Vertebrate ,Peixos ,Metabolisme ,Hemoglobin ,MD ,Computer Science Applications ,Cytoglobin-1 of D. mawsoni ,DTT ,030220 oncology & carcinogenesis ,Molecular Dynamics ,Mb ,C.aceCygb-1 ,Cytoglobin 1 ,Cygb-2 ,Cygbp, Penta-coordinated Cygb ,Engineering sciences. Technology ,Peroxynitrite ,Biotechnology ,Research Article ,Dissostichus ,RNS, Reactive Nitrogen Species ,lcsh:Biotechnology ,Biophysics ,MD, Molecular Dynamics ,Cygb, Cytoglobin ,DTT, Dithiothreitol ,Hb, Hemoglobin ,NO, Nitric oxide ,rms, Root-mean square ,03 medical and health sciences ,Cygbh, Hexa-coordinated bis-histidyl species ,D.mawCygb-1*, Mutant of D.mawCygb-1 ,lcsh:TP248.13-248.65 ,biology.animal ,Genetics ,Mutant of C.aceCygb-1 ,14. Life underwater ,Hexa-coordinated bis-histidyl species ,Cygbp ,D.mawCygb-1, Cytoglobin-1 of D. mawsoni ,Biology ,030304 developmental biology ,Biologia molecular ,C.aceCygb-1, Cytoglobin-1 of C. aceratus ,Ligand ,Carbon monoxide ,CYGB ,O2 partial pressure required to achieve half saturation ,rms ,CYGB, Human Cygb ,Enzyme kinetics ,Cygb-2, Cytoglobin 2 ,Mb, Myoglobin ,biology.organism_classification ,Enzyme ,Metabolism ,Cygb-1 ,Root-mean square ,Dithiothreitol ,Hb ,Genètica ,ROS, Reactive Oxygen Species - Abstract
Graphical abstract 1These authors contributed equally as First Author., 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.
- Published
- 2020