Neuroglobin, seven years after

Neuroglobin is expressed in vertebrates brain and belongs to a branch of the globin family that diverged early in evolution. Sequence conservation suggests a relevant role in the nervous system, with tight structural restraints. Experiments in vivo and in vitro showed increased hypoxic stress damage...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2007-05, Vol.64 (10), p.1259-1268
Main Authors: Brunori, M, Vallone, B
Format: Article
Language:English
Subjects:
Animals
Biosynthesis
Carbon Dioxide - metabolism
Crystallography
Erythrocytes
Evolution
Evolution, Molecular
Genetics
Globins
Globins - chemistry
Globins - genetics
Globins - metabolism
Hemoglobin
Humans
Hypoxia
ligand binding
Models, Molecular
Nerve Tissue Proteins - chemistry
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neuroglobin
neuroprotection
Oxygen
Oxygen - metabolism
Protein Binding
Protein Structure, Tertiary
radical scavenging
Review
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Summary:Neuroglobin is expressed in vertebrates brain and belongs to a branch of the globin family that diverged early in evolution. Sequence conservation suggests a relevant role in the nervous system, with tight structural restraints. Experiments in vivo and in vitro showed increased hypoxic stress damage upon repressing neuroglobin biosynthesis and improved recovery following overexpression. Neuroglobin shows internal heme hexacoordination, which controls oxygen affinity and kinetics. Neuroglobin concentration, oxygen affinity and enhanced autooxidation question a role in oxygen delivery; thus it was proposed that the neuroprotective effect might be due to radical scavenging or activation of protection mechanisms. Neuroglobin's structure shows a peculiar internal cavity of very large size. Binding of heme ligands is associated to a conformational change involving the heme that “slides” into the pre-existing cavity and makes the sixth coordination position available. These features may pave the way to an understanding of neuroprotection by neuroglobin.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-007-7090-2