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The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin
Open accessAbstract
Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well. The existence and position of these disulfide bonds was demonstrated by mass spectrometry and thiol accessibility studies. Mutation of the cysteines involved, or the use of reducing agents to break the S-S bond, led to a decrease in the observed oxygen affinity of human neuroglobin by an order of magnitude. The critical parameter is the histidine dissociation rate, which changes by about a factor of 10. The same effect is observed with human cytoglobin, although to a much lesser extent (less than a factor of 2). These results suggest a novel mechanism for the regulation of oxygen binding; contact with an appropriate electron donor would provoke the release of oxygen. Hence the oxygen affinity would be directly linked to the redox state of the cell.
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“neuroglobin will increase its penta-coordinated character upon oxidation of Cys46 and Cys55 to form a disulfide bond [64, 80-82].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [80]
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Metadata
- Authors
- Hamdane, D., Kiger, L., Dewilde, S., Green, B. N., Pesce, A., Uzan, J., Burmester, T., Hankeln, T., Bolognesi, M., Moens, L., & Marden, M. C.
- Affiliations
- Inserm (FR)
- University of Antwerp (BE)
- University of Genoa (IT)
- Johannes Gutenberg University Mainz (DE)
- Corresponding author
- Marden, Michael C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-12
- Volume
- 278
- Issue
- 51
- Pages
- 51713-51721
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2164923948
- Cited by
- 274
- References
- 38
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 3 · 2023: 11 · 2022: 10 · 2021: 8 · 2020: 8 · 2019: 8 · 2018: 11 · 2017: 14 · 2016: 13 · 2015: 12 · 2014: 11 · 2013: 15 · 2012: 8
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CINECA IRIS Institutial Research Information System (University of Genoa) (submittedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Funders
- European Commission (QLG3-CT-2002-01548)
- Deutsche Forschungsgemeinschaft (Ha2103/3, Bu956/5)
- Institut National de la Santé et de la Recherche Médicale
- Consiglio Nazionale delle Ricerche
- Universiteit Antwerpen
- Vlaamse regering
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- neuroglobin, cytoglobin, oxygen affinity, redox regulation, disulfide bonds, cysteine residues, distal histidine, reducing agents, electron donors
- MeSH terms
- Neuroglobin, Cytoglobin, Cysteine, Disulfides, Globins, Histidine, Humans, Kinetics, Ligands, Models, Molecular, Nerve Tissue Proteins, Oxidation-Reduction, Oxygen, Protein Binding, Recombinant Proteins, Spectrometry, Mass, Electrospray Ionization
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