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J. Biol. Chem., Vol. 276, Issue 32, 30326-30334, August 10, 2001
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From the Haemophilus ducreyi, the causative
agent of the genital ulcerative disease known as chancroid, is unable
to synthesize heme, which it acquires from humans, its only known host.
Here we provide evidence that the periplasmic Cu,Zn-superoxide
dismutase from this organism is a heme-binding protein, unlike all the
other known Cu,Zn-superoxide dismutases from bacterial and eukaryotic species. When the H. ducreyi enzyme was expressed in
Escherichia coli cells grown in standard LB medium, it
contained only limited amounts of heme covalently bound to the
polypeptide but was able efficiently to bind exogenously added hemin.
Resonance Raman and electronic spectra at neutral pH indicate that
H. ducreyi Cu,Zn-superoxide dismutase contains a
6-coordinated low spin heme, with two histidines as the most likely
axial ligands. By site-directed mutagenesis and analysis of a
structural model of the enzyme, we identified as a putative axial
ligand a histidine residue (His-64) that is present only in the
H. ducreyi enzyme and that was located at the bottom of the
dimer interface. The introduction of a histidine residue in the
corresponding position of the Cu,Zn-superoxide dismutase from
Haemophilus parainfluenzae was not sufficient to confer the
ability to bind heme, indicating that other residues neighboring His-64
are involved in the formation of the heme-binding pocket. Our results
suggest that periplasmic Cu,Zn-superoxide dismutase plays a role in
heme metabolism of H. ducreyi and provide further evidence
for the structural flexibility of bacterial enzymes of this class.
A Novel Heme Protein, the Cu,Zn-Superoxide Dismutase
from Haemophilus ducreyi*
,
,, and**
Dipartimento di Biologia and
INFM, Università di Roma Tor Vergata, Via della
Ricerca Scientifica, 00133 Roma, Italy, the § Molecular
Infectious Diseases Group, Department of Paediatrics, Imperial College
School of Medicine, St. Mary's Hospital, Norfolk Place,
London W2 1PG, United Kingdom, and the ¶ Dipartimento di
Chimica, Universita' di Firenze, Via G. Capponi 9, 50121 Firenze, Italy
*
This work was supported in part by the MURST-CNR program
L.95/95 "Biomolecole per la Salute Umana," the CNR target project on Biotechnology, The Wellcome Trust (to J. S. K. and P. R. L.), and by MURST.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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