Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes.

@article{Brunori2005NeuroglobinNO,
  title={Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes.},
  author={M. Brunori and A. Giuffr{\`e} and K. Nienhaus and G. Nienhaus and F. Scandurra and B. Vallone},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 24},
  pages={
          8483-8
        }
}
  • M. Brunori, A. Giuffrè, +3 authors B. Vallone
  • Published 2005
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
Neuroglobin (Ngb) is a globin expressed in the nervous system of humans and other organisms that is involved in the protection of the brain from ischemic damage. Despite considerable interest, however, the in vivo function of Ngb is still a conundrum. In this paper we report a number of kinetic experiments with O2 and NO that we have interpreted on the basis of the 3D structure of Ngb, now available for human and murine metNgb and murine NgbCO. The reaction of reduced deoxyNgb with O2 and NO is… Expand
Electrochemical Evidence for Neuroglobin Activity on NO at Physiological Concentrations*
TLDR
Electrochemical measurements were used to investigate the role of an intermittent internal disulfide bridge in determining NO oxidation kinetics at physiological NO concentrations and identified a role for the distal histidine, interacting with the hexacoordinated iron atom of the heme, in oxidation Kinetics. Expand
Neuroglobin: enzymatic reduction and oxygen affinity.
TLDR
A novel reduction protocol for metNgb based on NADH:flavorubredoxin oxidoreductase (FlRd-red) from Escherichia coli, a candidate for the Ngb reducing activity recently identified in E. coli extracts, is introduced. Expand
Reactivity and endogenous modification by nitrite and hydrogen peroxide: does human neuroglobin act only as a scavenger?
TLDR
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. Expand
A globin for the brain
  • M. Brunori, B. Vallone
  • Biology, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2006
TLDR
It appears that neuroglobin is a stress‐responsive sensor for signal transduction in the brain, mediated by a ligand‐linked conformational change of the protein. Expand
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TLDR
It is concluded that it is still too early to definitively decide what may be the physiological role(s) of neuroglobin in vertebrates, but there is no doubt that neuro globin has an essential, conserved function and is beneficial to neurons. Expand
Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration.
TLDR
Simulations based on this kinetic model suggest that the high efficiency of Cygb in regulating the NO consumption rate is due to the rapid reduction ofCygb by cellular reductants, which greatly increases the rate of consumption of NO at higher O(2) concentrations, and binding of NO to Cygb, which reduces the rates of consumption at lower O( 2) concentrations. Expand
Neuroglobin: From structure to function in health and disease.
TLDR
Structural and functional aspects of human Ngb are examined critically to highlight its roles in health and disease and opening new therapeutic approaches to prevent neuronal cell death. Expand
Reactions of ferrous neuroglobin and cytoglobin with nitrite under anaerobic conditions.
TLDR
It is found that nitric oxide dissociates from ferrous neuroglobin much faster than previously appreciated, consistently with the decay of the Fe(II)-NO product during the reaction. Expand
Neuroglobin and cytoglobin as potential enzyme or substrate.
TLDR
In vivo and in vitro studies show that Escherichia coli cells contain an enzymatic reducing system that keeps the heme iron atom of neuroglobin in the Fe(2+) form in the presence of dioxygen despite the high autoxidation rate of the molecule. Expand
Exploring the Mechanisms of the Reductase Activity of Neuroglobin by Site-Directed Mutagenesis of the Heme Distal Pocket
TLDR
A relationship between the nitrite reduction rate and heme accessibility in Ngb, particularly marked for His64(E7) mutants is suggested, which may be related to a differential stabilization of the iron–nitrite complexes in five- and six-coordinate globins. Expand
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