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J. Biol. Chem., Vol. 278, Issue 7, 4919-4925, February 14, 2003
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From the Departments of Neuroglobin is a recently discovered member of
the globin superfamily. Combined electron paramagnetic resonance
and optical measurements show that, in Escherichia coli
cell cultures with low O2 concentration overexpressing
wild-type mouse recombinant neuroglobin, the heme protein is mainly in
a hexacoordinated deoxy ferrous form (F8His-Fe2+-E7His),
whereby for a small fraction of the protein the endogenous protein
ligand is replaced by NO. Analogous studies for mutated neuroglobin
(mutation of E7-His to Leu, Val, or Gln) reveal the predominant
presence of the nitrosyl ferrous form. After sonication of the cells
wild-type neuroglobin oxidizes rapidly to the hexacoordinated ferric
form, whereas NO ligation initially protects the mutants from
oxidation. Flash photolysis studies of wild-type neuroglobin and its E7
mutants show high recombination rates (kon) and
low dissociation rates (koff) for NO,
indicating a high intrinsic affinity for this ligand similar to that of
other hemoglobins. Since the rate-limiting step in ligand combination
with the deoxy-hexacoordinated wild-type form involves the dissociation
of the protein ligand, NO binding is slower than for the related
mutants. Structural and kinetic characteristics of neuroglobin
and its mutants are analyzed. NO production in rapidly growing E. coli cell cultures is discussed.
Nitric Oxide Binding Properties of Neuroglobin
A CHARACTERIZATION BY EPR AND FLASH PHOTOLYSIS*,
,
,**,,, and
Physics and ¶ Biomedical
Sciences, University of Antwerp, B-2610 Antwerp, Belgium,
INSERM, Unite 473, Hôpital de Bicètre, F94275 Le
Kremlin- Bicètre, France, and the ** National Institute
for Materials Physics, POB MG-7 Magurele-Bucuresti, Romania
*
This work was supported in part by Fund for Scientific
Research-Flanders (FWO) Grant G.0409.02 (to E. G.) and Grant
QLRT-2001-01548 from the European Union.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.
The on-line version of this article (available at
http://www.jbc.org) contains supplementary figures and data.
§
Postdoctoral fellow from the FWO. To whom correspondence should be
addressed: Dept. of Physics, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium. Tel.: 0032-3-8202461; Fax: 0032-3-8202470; E-mail: Sabine.VanDoorslaer@ua.ac.be.
Supported by Grant G.0069.98 from the FWO.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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