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J. Biol. Chem., Vol. 276, Issue 42, 38949-38955, October 19, 2001
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From the Neuroglobin is a recently discovered member of
the globin superfamily that is suggested to enhance the
O2 supply of the vertebrate brain. Spectral
measurements with human and mouse recombinant neuroglobin provide
evidence for a hexacoordinated deoxy ferrous (Fe2+) form,
indicating a His-Fe2+-His binding scheme. O2 or
CO can displace the endogenous protein ligand, which is identified as
the distal histidine by mutagenesis. The ferric (Fe3+) form
of neuroglobin is also hexacoordinated with the protein ligand E7-His
and does not exhibit pH dependence. Flash photolysis studies show a
high recombination rate (kon) and a slow
dissociation rate (koff) for both
O2 and CO, indicating a high intrinsic affinity for these
ligands. However, because the rate-limiting step in ligand combination
with the deoxy hexacoordinated form involves the dissociation of the
protein ligand, O2 and CO binding is suggested to be slow
in vivo. Because of this competition, the observed O2 affinity of recombinant human neuroglobin is average (1 torr at 37 °C). Neuroglobin has a high autoxidation rate, resulting in an oxidation at 37 °C by air within a few minutes. The
oxidation/reduction potential of mouse neuroglobin
(E'o =
Biochemical Characterization and Ligand Binding
Properties of Neuroglobin, a Novel Member of the Globin Family*
§¶,
,
,
,
,
,
¶¶
Department of Biochemistry, University of
Antwerp, B-2610 Antwerp, Belgium,
INSERM, Unite 473, Hôpital de Bicètre, F94275 Le Kremlin-Bicètre,
France, the ** Institute of Zoology, Johannes Gutenberg
University of Mainz, D-55099 Mainz, Germany, the

Institute of Molecular Genetics, Biosafety
Research and Consulting, Johannes Gutenberg University of Mainz,
D-55099 Mainz, Germany, and the §§ Department of
Biology, University of Antwerp, B-2610 Antwerp, Belgium
129 mV) lies within the physiological
range. Under natural conditions, recombinant mouse neuroglobin occurs
as a monomer with disulfide-dependent formation of dimers.
The biochemical and kinetic characteristics are discussed in view of
the possible functions of neuroglobin in the vertebrate brain.
*
This work was supported in part by funds from INSERM,
Association Recherche et Transfusion Contract 21-2000, by a
collaboration of University and INSERM, and by Deutsche
Forschungsgemeinschaft Grant Ha3201/3;Bu956/3.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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