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Giordano D, Pesce A, Vermeylen S, et al. Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions. Comput Struct Biotechnol J. 2020;18:2132-2144doi: 10.1016/j.csbj.2020.08.007.
Giordano, D., Pesce, A., Vermeylen, S., Abbruzzetti, S., Nardini, M., Marchesani, F., Berghmans, H., Seira, C., Bruno, S., Javier Luque, F., di Prisco, G., Ascenzi, P., Dewilde, S., Bolognesi, M., Viappiani, C., & Verde, C. (2020). Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions. Computational and structural biotechnology journal, 182132-2144. https://doi.org/10.1016/j.csbj.2020.08.007
Giordano, Daniela, et al. "Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions." Computational and structural biotechnology journal vol. 18 (2020): 2132-2144. doi: https://doi.org/10.1016/j.csbj.2020.08.007
Giordano D, Pesce A, Vermeylen S, Abbruzzetti S, Nardini M, Marchesani F, Berghmans H, Seira C, Bruno S, Javier Luque F, di Prisco G, Ascenzi P, Dewilde S, Bolognesi M, Viappiani C, Verde C. Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions. Comput Struct Biotechnol J. 2020 Aug 12;18:2132-2144. doi: 10.1016/j.csbj.2020.08.007. eCollection 2020. PMID: 32913582; PMCID: PMC7451756.
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Comput Struct Biotechnol J. 2020 Aug 12;18:2132-2144. doi: 10.1016/j.csbj.2020.08.007. eCollection 2020.

Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions.

Computational and structural biotechnology journal

Daniela Giordano, Alessandra Pesce, Stijn Vermeylen, Stefania Abbruzzetti, Marco Nardini, Francesco Marchesani, Herald Berghmans, Constantí Seira, Stefano Bruno, F Javier Luque, Guido di Prisco, Paolo Ascenzi, Sylvia Dewilde, Martino Bolognesi, Cristiano Viappiani, Cinzia Verde

Affiliations

  1. Institute of Biosciences and BioResources (IBBR), CNR, Via Pietro Castellino 111 80131 Napoli, Italy.
  2. Department of Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121 Napoli, Italy.
  3. Department of Physics, University of Genova, Via Dodecaneso 33, I-16121 Genova, Italy.
  4. Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, B-2610 Wilrijk, Belgium.
  5. Department of Mathematical, Physical and Computer Sciences, University of Parma, Parco Area delle Scienze 7A, 43124 Parma, Italy.
  6. Department of Biosciences, University of Milano, Via Celoria 26, I-20133 Milano, Italy.
  7. Department of Food and Drug, University of Parma, Parco Area delle Scienze 23A, 43124, Parma, Italy.
  8. Department of Nutrition, Food Science and Gastronomy, Faculty of Pharmacy and Food Science, Institute of Biomedicine (IBUB) and Institute of Theoretical and Computational Chemistry (IQTCUB), University of Barcelona, Av. Prat de la Riba 171, Santa Coloma de Gramenet E-08921, Spain.
  9. Interdepartmental Laboratory for Electron Microscopy, Roma Tre University, Via della Vasca Navale 79, I-00146 Roma, Italy.

PMID: 32913582 PMCID: PMC7451756 DOI: 10.1016/j.csbj.2020.08.007

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,

© 2020 The Authors.

Keywords: C.aceCygb-1*, Mutant of C.aceCygb-1; C.aceCygb-1, Cytoglobin-1 of C. aceratus; CO, Carbon monoxide; CYGB, Human Cygb; Cold-adaptation; Cygb, Cytoglobin; Cygb-1, Cytoglobin 1; Cygb-2, Cytoglobin 2; Cygbh, Hexa-coordinated bis-histidyl species; Cygbp, Penta-coordinated Cygb; Cytoglobin; D.mawCygb-1*, Mutant of D.mawCygb-1; D.mawCygb-1, Cytoglobin-1 of D. mawsoni; DTT, Dithiothreitol; Hb, Hemoglobin; Ligand properties; MD, Molecular Dynamics; Mb, Myoglobin; NGB, Human neuroglobin; NO dioxygenase; NO, Nitric oxide; RNS, Reactive Nitrogen Species; ROS, Reactive Oxygen Species; X-ray structure; p50, O2 partial pressure required to achieve half saturation; rms, Root-mean square

Conflict of interest statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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