ArticleBiochemistry2008
Identification of protein radicals formed in the human neuroglobin-H2O2 reaction using immuno-spin trapping and mass spectrometry.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Engineering a highly selective, hemoprotein-based scavenger as a carbon monoxide poisoning antidote with no hypertensive effect.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin.Bioscience reports · 2025Article
- Peroxidase activity of rice (Oryza sativa) hemoglobin: distinct role of tyrosines 112 and 151.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Hydrogen peroxide induces heme degradation and protein aggregation in human neuroglobin: roles of the disulfide bridge and hydrogen-bonding in the distal heme cavity.The FEBS journal · 2023Article
- Emerging perspectives on cytoglobin, beyond NO dioxygenase and peroxidase.Redox biology · 2020Review
- Article
- Immuno-spin trapping from biochemistry to medicine: advances, challenges, and pitfalls. Focus on protein-centered radicals.Biochimica et biophysica acta · 2014Review
- Ultraviolet laser-induced cross-linking in peptides.Rapid communications in mass spectrometry : RCM · 2013Article
- Crucial roles of Glu60 in human neuroglobin as a guanine nucleotide dissociation inhibitor and neuroprotective agent.PloS one · 2013Article
- Recycling of the high valence States of heme proteins by cysteine residues of THIMET-oligopeptidase.PloS one · 2013Article
- Detection of Ras GTPase protein radicals through immuno-spin trapping.Free radical biology & medicine · 2012Article
- Human neuroglobin functions as an oxidative stress-responsive sensor for neuroprotection.The Journal of biological chemistry · 2012Article
- Regulation of Ras proteins by reactive nitrogen species.Free radical biology & medicine · 2011Review
- Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Neuroglobin and cytoglobin: two new members of globin family.Revista brasileira de hematologia e hemoterapia · 2011Article
- Biotinylated analogue of the spin-trap 5,5-dimethyl-1-pyrroline-N-oxide for the detection of low-abundance protein radicals by mass spectrometry.Analytical chemistry · 2010Article
- Neuroglobin protects neurons against oxidative stress in global ischemia.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2010Article
- Iron-mediated oxidation induces conformational changes within the redox-sensing protein HbpS.The Journal of biological chemistry · 2010Article
- Neuroglobin genetic polymorphisms and their relationship to functional outcomes after traumatic brain injury.Journal of neurotrauma · 2010Article
- Immuno-spin trapping of protein and DNA radicals: "tagging" free radicals to locate and understand the redox process.Free radical biology & medicine · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Neuroglobin (Ngb) is a recently discovered protein that shows only minor sequence similarity with myoglobin and hemoglobin but conforms to the typical 3-over-3 alpha-helical fold characteristic of vertebrate globins. An intriguing feature of Ngb is its heme hexacoordination in the absence of external ligands, observed both in the ferrous and in the ferric (met) forms. In Ngb, the imidazole of a histidine residue (His-64) in the distal position, above the heme plane, provides the sixth coordination bond. In this work, a valine residue was introduced at position 64 (H64V variant) to clarify the possible role(s) of the distal residue in protecting the heme iron of Ngb from attack by strong oxidants. SDS-PAGE analyses revealed that the oxidation of the H64V variant of metNgb by H 2O 2 resulted in the formation of dimeric and trimeric products in contrast to the native protein. Dityrosine cross-links were shown by their fluorescence to be present in the oligomeric products. When the spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) was included in the reaction mixture, nitrone adducts were detected by immuno-spin trapping. The specific location of the DMPO adducts on the H64V variant protein was determined by a mass spectrometry method that combines off-line immuno-spin trapping and chromatographic procedures. This method revealed Tyr-88 to be the site of modification by DMPO. The presence of His-64 in the wild-type protein results in the nearly complete loss of detectable radical adducts. Together, the data support the argument that wild-type Ngb is protected from attack by H 2O 2 by the coordinated distal His.
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