| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 32, 30326-30334, August 10, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,
,, and**
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.
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
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  N. V. Balashova, D. H. Park, J. K. Patel, D. H. Figurski, and S. C. Kachlany Interaction between Leukotoxin and Cu,Zn Superoxide Dismutase in Aggregatibacter actinomycetemcomitans Infect. Immun., September 1, 2007; 75(9): 4490 - 4497. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Krishnakumar, B. Kim, E. A. Mollo, J. A. Imlay, and J. M. Slauch Structural Properties of Periplasmic SodCI That Correlate with Virulence in Salmonella enterica Serovar Typhimurium J. Bacteriol., June 15, 2007; 189(12): 4343 - 4352. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. M. B. Post, R. Mungur, B. W. Gibson, and R. S. Munson Jr. Identification of a Novel Sialic Acid Transporter in Haemophilus ducreyi Infect. Immun., October 1, 2005; 73(10): 6727 - 6735. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. T. H. Bong, K. R. Fortney, B. P. Katz, A. F. Hood, L. R. S. Mateo, T. H. Kawula, and S. M. Spinola A Superoxide Dismutase C Mutant of Haemophilus ducreyi Is Virulent in Human Volunteers Infect. Immun., March 1, 2002; 70(3): 1367 - 1371. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Battistoni, F. Pacello, A. P. Mazzetti, C. Capo, J. S. Kroll, P. R. Langford, A. Sansone, G. Donnarumma, P. Valenti, and G. Rotilio A Histidine-rich Metal Binding Domain at the N Terminus of Cu,Zn-Superoxide Dismutases from Pathogenic Bacteria. A NOVEL STRATEGY FOR METAL CHAPERONING J. Biol. Chem., August 3, 2001; 276(32): 30315 - 30325. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
