Antarctic fish versus human cytoglobins -- The same but yet
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TitleAntarctic fish versus human cytoglobins -- The same but yet so differentAbstractThe cytoglobins of the Antarctic fish Chaenocephalus aceratus and Dissostichus mawsoni have many features in common with human cytoglobin. These cytoglobins are heme proteins in which the ferric and ferrous forms have a characteristic hexacoordination of the heme iron, i.e. axial ligation of two endogenous histidine residues, as confirmed by electron paramagnetic resonance, resonance Raman and optical absorption spectroscopy. The combined spectroscopic analysis revealed only small variations in the heme-pocket structure, in line with the small variations observed for the redox potential. Nevertheless, some striking differences were also discovered. Resonance Raman spectroscopy showed that the stabilization of an exogenous heme ligand, such as CO, occurs differently in human cytoglobin in comparison with Antarctic fish cytoglobins. Furthermore, while it has been extensively reported that human cytoglobin is essentially monomeric and can form an intramolecular disulfide bridge that can influence the ligand binding kinetics, 3D modeling of the Antarctic fish cytoglobins indicates that the cysteine residues are too far apart to form such an intramolecular bridge. Moreover, gel filtration and mass spectrometry reveal the occurrence of non-covalent multimers (up to pentamers) in the Antarctic fish cytoglobins that are formed at low concentrations. Stabilization of these oligomers by disulfide-bridge formation is possible, but not essential. If intermolecular disulfide bridges are formed, they influence the heme-pocket structure, as is shown by EPR measurements. â"' 2017 Elsevier Inc.AcknowledgementsThe authors acknowledge the support of the University of Antwerp GOA-BOF funding (28312), FWO funding (G.0687.13) and the Hercules foundation for funding of the Synapt G2 instrument. This study was carried out in the framework of the SCAR program Ãntarctic Thresholds -- Ecosystem Resilience and Adaptation Ì(AnT-ERA). It was financially supported by the Italian National Program for Antarctic Research (PNRA). Research of A. De Schutter is funded by a PhD grant of the Agency for Innovation by Science and Technology (121339) (IWT, Belgium). C-H C. Cheng acknowledges funding support from US National Science Foundation Polar Programs (ANT-1142158). The authors acknowledge C-H C. Cheng and P. Cziko for the picture of a D. mawsoni that is used in the graphical abstract.Funding Details28312, Universiteit Antwerpen; G.0687.13, Universiteit Antwerpen
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1st AuthorCuypers, B.AuthorCuypers, B.Vermeylen, S.Hammerschmid, D.Trashin, S.Rahemi, V.Konijnenberg, A.De Schutter, A.Cheng, C.-H.Giordano, D.Verde, C.De Wael, K.Sobott, F.Dewilde, S.Van Doorslaer, S.Year2017JournalJournal of Inorganic BiochemistryVolume173Pages66-78DOI10.1016/j.jinorgbio.2017.04.025URLhttps://www.scopus.com/inward/recor.....09839fc217d82409a04265b25Author KeywordsCytoglobinElectron paramagnetic resonanceMass spectrometryProtein expressionRedoxResonance Raman spectroscopy
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TypeArticleCitationCuypers, B., Vermeylen, S., Hammerschmid, D., Trashin, S., Rahemi, V., Konijnenberg, A., De Schutter, A., Cheng, C.-H., Giordano, D., Verde, C., De Wael, K., Sobott, F., Dewilde, S. and Van Doorslaer, S. (2017). Antarctic fish versus human cytoglobins -- The same but yet so different. Journal of Inorganic Biochemistry, 173: 66-78 IdentifierCuypers2017Antarctica NZ supported?NoNZARI?No
Van Doorslaer, S., Antarctic fish versus human cytoglobins -- The same but yet , [Cuypers2017]. Antarctica NZ, accessed 02/08/2026, https://adam.antarcticanz.govt.nz/nodes/view/63459, 10.1016/j.jinorgbio.2017.04.025