ArticleThe Journal of biological chemistry2016
Electrochemical Evidence for Neuroglobin Activity on NO at Physiological Concentrations.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Cytochrome bFree radical biology & medicine · 2026Article
- Insights into the Function of a Conserved Cys120 in Human Neuroglobin in Oxidative Stress Regulation of Breast Cancer Cells.Biomolecules · 2026Article
- Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin.Bioscience reports · 2025Article
- 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
- Ordered Motions in the Nitric-Oxide Dioxygenase Mechanism of Flavohemoglobin and Assorted Globins with Tightly Coupled Reductases.Advances in experimental medicine and biology · 2023Article
- Carbon Monoxide Signaling: Examining Its Engagement with Various Molecular Targets in the Context of Binding Affinity, Concentration, and Biologic Response.Pharmacological reviews · 2022Review
- Structural and (Pseudo-)Enzymatic Properties of Neuroglobin: Its Possible Role in Neuroprotection.Cells · 2021Review
- Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin.RSC advances · 2019Article
- Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome bBiochemistry · 2017Article
- Neuroglobin Can Prevent or Reverse Glaucomatous Progression in DBA/2J Mice.Molecular therapy. Methods & clinical development · 2017Article
- Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.Scientific reports · 2017Article
- Neuroglobin, a Factor Playing for Nerve Cell Survival.International journal of molecular sciences · 2016Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The true function of neuroglobin (Ngb) and, particularly, human Ngb (NGB) has been under debate since its discovery 15 years ago. It has been expected to play a role in oxygen binding/supply, but a variety of other functions have been put forward, including NO dioxygenase activity. However, in vitro studies that could unravel these potential roles have been hampered by the lack of an Ngb-specific reductase. In this work, we used electrochemical measurements to investigate the role of an intermittent internal disulfide bridge in determining NO oxidation kinetics at physiological NO concentrations. The use of a polarized electrode to efficiently interconvert the ferric (Fe(3+)) and ferrous (Fe(2+)) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB. Our studies further identified a role for the distal histidine, interacting with the hexacoordinated iron atom of the heme, in oxidation kinetics. These findings may be relevant in vivo, for example, in blocking apoptosis by reduction of ferric cytochrome c, and gentle tuning of NO concentration in the tissues.
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