Reactivity and endogenous modification by nitrite and hydrogen peroxide: does human neuroglobin act only as a scavenger?
Open accessAbstract
NGB (human neuroglobin), a recently discovered haem protein of the globin family containing a six-co-ordinated haem, is expressed in nervous tissue, but the physiological function of NGB is currently unknown. As well as playing a role in neuronal O2 homoeostasis, NGB is thought to act as a scavenger of reactive species. In the present study, we report on the reactivity of metNGB (ferric-NGB), which accumulates in vivo as a result of the reaction of oxyNGB (oxygenated NGB) with NO, towards NO2- and H2O2. NO2- co-ordination of the haem group accounts for the activity of metNGB in the nitration of phenolic substrates. The two different metNGB forms, with and without the internal disulfide bond between Cys46 (seventh residue on the inter-helix region between helices C and D) and Cys55 (fifth residue on helix D), exhibit different reactivity, the former being more efficient in activating NO2-. The kinetics of the reactions, the NO2--binding studies and the analysis of the nitrated products from different substrates all support the hypothesis that metNGB is able to generate an active species with the chemical properties of peroxynitrite, at pathophysiological concentrations of NO2- and H2O2. Without external substrates, the targets of the reactive species generated by the metNGB/NO2-/H2O2 system are endogenous tyrosine (resulting in the production of 3-nitrotyrosine) and cysteine (oxidized to sulfinic acid and sulfonic acid) residues. These endogenous modifications were characterized by HPLC-MS/MS (tandem MS) analysis of metNGB after reaction with NO2- and H2O2 under various conditions. The internal S-S bond affects the functional properties of the protein. Therefore metNGB acts not only as scavenger of toxic species, but also as a target of the self-generated reactive species. Self-modification of the protein may be related to or inhibit its postulated neuroprotective activity.
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Neuroglobin increases its penta-coordinated character upon oxidation of Cys46 and Cys55 to form a disulfide bond.
“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 [82]
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Protein self‐modification by heme‐generated reactive species
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Self-citationImpact of A90P, F106L and H64V mutations on neuroglobin stability and ligand binding kinetics
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Neuroglobin deficiency increases seizure susceptibility but does not affect basal behavior in mice
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Biological Oxidations and Nitrations Promoted by the Hemin–Aβ16 Complex
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- Authors
- Nicolis, S., Monzani, E., Ciaccio, C., Ascenzi, P., Moens, L., & Casella, L.
- Affiliations
- University of Pavia (IT)
- University of Rome Tor Vergata (IT)
- Roma Tre University (IT)
- University of Antwerp (BE)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-09-12
- Volume
- 407
- Issue
- 1
- Pages
- 89-99
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2267408
- OpenAlex
- W2034762716
- Cited by
- 63
- References
- 53
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 1 · 2023: 5 · 2022: 6 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 4 · 2015: 2 · 2014: 4 · 2013: 3 · 2012: 1
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Funders
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Università degli Studi di Pavia
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- neuroglobin, nitrite, hydrogen peroxide, peroxynitrite, haem proteins, nitration, nitrotyrosine, cysteine oxidation, disulfide bonds, reactive oxygen species scavenging, neuroprotection, nitric oxide
- MeSH terms
- Neuroglobin, Amino Acid Sequence, Binding Sites, Catalysis, Cysteine, Disulfides, Globins, Humans, Hydrogen Peroxide, Kinetics, Models, Molecular, Molecular Sequence Data, Myoglobin, Nerve Tissue Proteins, Nitrites, Oxidation-Reduction, Phenols, Phenylacetates, Protein Conformation, Phenol, Tandem Mass Spectrometry
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