Antarctic fish versus human cytoglobins : the same but yet so different
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...
Published in: | Journal of Inorganic Biochemistry |
---|---|
Main Authors: | , , , , , , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2017
|
Subjects: | |
Online Access: | https://hdl.handle.net/10067/1448260151162165141 |
id |
ftunivantwerpen:c:irua:144826 |
---|---|
record_format |
openpolar |
spelling |
ftunivantwerpen:c:irua:144826 2024-10-06T13:44:23+00:00 Antarctic fish versus human cytoglobins : the same but yet so different Cuypers, Bert Vermeylen, Stijn Hammerschmid, Dietmar Trashin, Stanislav Rahemi, Vanousheh Konijnenberg, Albert De Schutter, Amy Cheng, C. -H. Christina Giordano, Daniela Verde, Cinzia De Wael, Karolien Sobott, Frank Dewilde, Sylvia Van Doorslaer, Sabine 2017 https://hdl.handle.net/10067/1448260151162165141 eng eng info:eu-repo/semantics/altIdentifier/doi/10.1016/J.JINORGBIO.2017.04.025 info:eu-repo/semantics/altIdentifier/isi/000405159600007 info:eu-repo/semantics/closedAccess 0162-0134 Journal of inorganic biochemistry Chemistry Biology info:eu-repo/semantics/article 2017 ftunivantwerpen https://doi.org/10.1016/J.JINORGBIO.2017.04.025 2024-09-10T04:06:38Z 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. Article in Journal/Newspaper Antarc* Antarctic IRUA - Institutional Repository van de Universiteit Antwerpen Antarctic The Antarctic Journal of Inorganic Biochemistry 173 66 78 |
institution |
Open Polar |
collection |
IRUA - Institutional Repository van de Universiteit Antwerpen |
op_collection_id |
ftunivantwerpen |
language |
English |
topic |
Chemistry Biology |
spellingShingle |
Chemistry Biology Cuypers, Bert Vermeylen, Stijn Hammerschmid, Dietmar Trashin, Stanislav Rahemi, Vanousheh Konijnenberg, Albert De Schutter, Amy Cheng, C. -H. Christina Giordano, Daniela Verde, Cinzia De Wael, Karolien Sobott, Frank Dewilde, Sylvia Van Doorslaer, Sabine Antarctic fish versus human cytoglobins : the same but yet so different |
topic_facet |
Chemistry Biology |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Cuypers, Bert Vermeylen, Stijn Hammerschmid, Dietmar Trashin, Stanislav Rahemi, Vanousheh Konijnenberg, Albert De Schutter, Amy Cheng, C. -H. Christina Giordano, Daniela Verde, Cinzia De Wael, Karolien Sobott, Frank Dewilde, Sylvia Van Doorslaer, Sabine |
author_facet |
Cuypers, Bert Vermeylen, Stijn Hammerschmid, Dietmar Trashin, Stanislav Rahemi, Vanousheh Konijnenberg, Albert De Schutter, Amy Cheng, C. -H. Christina Giordano, Daniela Verde, Cinzia De Wael, Karolien Sobott, Frank Dewilde, Sylvia Van Doorslaer, Sabine |
author_sort |
Cuypers, Bert |
title |
Antarctic fish versus human cytoglobins : the same but yet so different |
title_short |
Antarctic fish versus human cytoglobins : the same but yet so different |
title_full |
Antarctic fish versus human cytoglobins : the same but yet so different |
title_fullStr |
Antarctic fish versus human cytoglobins : the same but yet so different |
title_full_unstemmed |
Antarctic fish versus human cytoglobins : the same but yet so different |
title_sort |
antarctic fish versus human cytoglobins : the same but yet so different |
publishDate |
2017 |
url |
https://hdl.handle.net/10067/1448260151162165141 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
0162-0134 Journal of inorganic biochemistry |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/J.JINORGBIO.2017.04.025 info:eu-repo/semantics/altIdentifier/isi/000405159600007 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1016/J.JINORGBIO.2017.04.025 |
container_title |
Journal of Inorganic Biochemistry |
container_volume |
173 |
container_start_page |
66 |
op_container_end_page |
78 |
_version_ |
1812182784282722304 |