| Record |
| Author |
Cuypers, B.; Vermeylen, S.; Hammerschmid, D.; Trashin, S.; Rahemi, V.; Konijnenberg, A.; De Schutter, A.; Cheng, C.-H.C.; Giordano, D.; Verde, C.; De Wael, K.; Sobott, F.; Dewilde, S.; Van Doorslaer, S. |
| Title |
Antarctic fish versus human cytoglobins : the same but yet so different |
Type |
A1 Journal article |
Year  |
2017 |
Publication |
Journal of inorganic biochemistry |
Abbreviated Journal |
J Inorg Biochem |
| Volume |
173 |
Issue |
|
Pages |
66-78 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
| Abstract |
The 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. |
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Place of Publication |
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Editor |
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| Language |
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Wos |
000405159600007 |
Publication Date |
2017-04-28 |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0162-0134 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
| Impact Factor |
3.348 |
Times cited |
7 |
Open Access |
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| Notes |
; The 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 “Antarctic Thresholds – Ecosystem Resilience and Adaptation” (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). ; |
Approved |
Most recent IF: 3.348 |
| Call Number |
UA @ admin @ c:irua:144826 |
Serial |
5474 |
| Permanent link to this record |
