|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 275, Issue 37, 28439-28448, September 15, 2000
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Treponema pallidum, the
causative agent of venereal syphilis, is a microaerophilic obligate
pathogen of humans. As it disseminates hematogenously and invades a
wide range of tissues, T. pallidum presumably must tolerate
substantial oxidative stress. Analysis of the T. pallidum
genome indicates that the syphilis spirochete lacks most of the
iron-binding proteins present in many other bacterial pathogens,
including the oxidative defense enzymes superoxide dismutase, catalase,
and peroxidase, but does possess an orthologue (TP0823) for
neelaredoxin, an enzyme of hyperthermophilic and sulfate-reducing
anaerobes shown to possess superoxide reductase activity. To analyze
the potential role of neelaredoxin in treponemal oxidative defense, we
examined the biochemical, spectroscopic, and antioxidant properties of
recombinant T. pallidum neelaredoxin. Neelaredoxin was
shown to be expressed in T. pallidum by reverse transcriptase-polymerase chain reaction and Western blot analysis. Recombinant neelaredoxin is a 26-kDa
Neelaredoxin, an Iron-binding Protein from the Syphilis
Spirochete, Treponema pallidum, Is a Superoxide
Reductase*
§,
,,,,,, and§§§
Section of Hematology Research,
§ Department of Biochemistry and Molecular Biology, and
Biomedical Mass Spectrometry and Functional
Proteomics Facility, Mayo Clinic, Rochester, Minnesota 55905, the
¶ Departmento de Química and Centro de Química
Fina e Biotecnologia, Faculdade de Ciéncias e Tecnologia,
Universidade Nova de Lisboa, 2825 Monte de Caparica, Portugal, the
Department of Medicine and the Center for Microbial
Pathogenesis, University of Connecticut Health Center, MC3710,
Farmington, Connecticut 06030, and the ** Department of Physics, Emory
University, Atlanta, Georgia 30322
2 homodimer
containing, on average, 0.7 iron atoms/subunit. Mössbauer and EPR
analysis of the purified protein indicates that the iron atom exists as a mononuclear center in a mixture of high spin ferrous and ferric oxidation states. The fully oxidized form, obtained by the addition of
K3(Fe(CN)6), exhibits an optical spectrum with
absorbances at 280, 320, and 656 nm; the last feature is responsible
for the protein's blue color, which disappears upon ascorbate
reduction. The fully oxidized protein has a
A280/A656 ratio of
10.3. Enzymatic studies revealed that T. pallidum
neelaredoxin is able to catalyze a redox equilibrium between superoxide
and hydrogen peroxide, a result consistent with it being a superoxide
reductase. This finding, the first description of a T. pallidum iron-binding protein, indicates that the syphilis
spirochete copes with oxidative stress via a primitive mechanism,
which, thus far, has not been described in pathogenic bacteria.
*
This work was supported by National Institutes of Health
Grants AI 26756 (to J. D. R.) and GM58778 (to B. H. H.), by PRAXIS XXI (to C. A., I. M., and J. J. G. M.), and by support from the Mayo Foundation.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 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Kawasaki, Y. Sakai, T. Takahashi, I. Suzuki, and Y. Niimura O2 and Reactive Oxygen Species Detoxification Complex, Composed of O2-Responsive NADH:Rubredoxin Oxidoreductase-Flavoprotein A2-Desulfoferrodoxin Operon Enzymes, Rubperoxin, and Rubredoxin, in Clostridium acetobutylicum Appl. Envir. Microbiol., February 15, 2009; 75(4): 1021 - 1029. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Mathe, C. O. Weill, T. A. Mattioli, C. Berthomieu, C. Houee-Levin, E. Tremey, and V. Niviere Assessing the Role of the Active-site Cysteine Ligand in the Superoxide Reductase from Desulfoarculus baarsii J. Biol. Chem., July 27, 2007; 282(30): 22207 - 22216. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Zhu, X. Fu, Y. D. Koo, J.-K. Zhu, F. E. Jenney Jr., M. W. W. Adams, Y. Zhu, H. Shi, D.-J. Yun, P. M. Hasegawa, et al. An Enhancer Mutant of Arabidopsis salt overly sensitive 3 Mediates both Ion Homeostasis and the Oxidative Stress Response Mol. Cell. Biol., July 15, 2007; 27(14): 5214 - 5224. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. K. Deka, C. A. Brautigam, F. L. Tomson, S. B. Lumpkins, D. R. Tomchick, M. Machius, and M. V. Norgard Crystal Structure of the Tp34 (TP0971) Lipoprotein of Treponema pallidum: IMPLICATIONS OF ITS METAL-BOUND STATE AND AFFINITY FOR HUMAN LACTOFERRIN J. Biol. Chem., February 23, 2007; 282(8): 5944 - 5958. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. E. LaFond and S. A. Lukehart Biological Basis for Syphilis Clin. Microbiol. Rev., January 1, 2006; 19(1): 29 - 49. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Kawasaki, Y. Watamura, M. Ono, T. Watanabe, K. Takeda, and Y. Niimura Adaptive Responses to Oxygen Stress in Obligatory Anaerobes Clostridium acetobutylicum and Clostridium aminovalericum Appl. Envir. Microbiol., December 1, 2005; 71(12): 8442 - 8450. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. M. Grunden, F. E. Jenney Jr., K. Ma, M. Ji, M. V. Weinberg, and M. W. W. Adams In Vitro Reconstitution of an NADPH-Dependent Superoxide Reduction Pathway from Pyrococcus furiosus Appl. Envir. Microbiol., March 1, 2005; 71(3): 1522 - 1530. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Seshadri, G. S. A. Myers, H. Tettelin, J. A. Eisen, J. F. Heidelberg, R. J. Dodson, T. M. Davidsen, R. T. DeBoy, D. E. Fouts, D. H. Haft, et al. Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes PNAS, April 13, 2004; 101(15): 5646 - 5651. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. L. T. O. Nascimento, A. I. Ko, E. A. L. Martins, C. B. Monteiro-Vitorello, P. L. Ho, D. A. Haake, S. Verjovski-Almeida, R. A. Hartskeerl, M. V. Marques, M. C. Oliveira, et al. Comparative Genomics of Two Leptospira interrogans Serovars Reveals Novel Insights into Physiology and Pathogenesis J. Bacteriol., April 1, 2004; 186(7): 2164 - 2172. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Emerson, E. D. Coulter, R. S. Phillips, and D. M. Kurtz Jr. Kinetics of the Superoxide Reductase Catalytic Cycle J. Biol. Chem., October 10, 2003; 278(41): 39662 - 39668. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. R. O. Hazlett, F. Rusnak, D. G. Kehres, S. W. Bearden, C. J. La Vake, M. E. La Vake, M. E. Maguire, R. D. Perry, and J. D. Radolf The Treponema pallidum tro Operon Encodes a Multiple Metal Transporter, a Zinc-dependent Transcriptional Repressor, and a Semi-autonomously Expressed Phosphoglycerate Mutase J. Biol. Chem., May 30, 2003; 278(23): 20687 - 20694. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. P. Emerson, D. E. Cabelli, and D. M. Kurtz Jr. Bioinorganic Chemistry Special Feature: An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and invivo PNAS, April 1, 2003; 100(7): 3802 - 3807. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I. A. Abreu, L. M. Saraiva, C. M. Soares, M. Teixeira, and D. E. Cabelli The Mechanism of Superoxide Scavenging by Archaeoglobus fulgidus Neelaredoxin J. Biol. Chem., October 12, 2001; 276(42): 38995 - 39001. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. R.O. Hazlett, T. J. Sellati, T. T. Nguyen, D. L. Cox, M. L. Clawson, M. J. Caimano, and J. D. Radolf The TprK Protein of Treponema pallidum Is Periplasmic and Is Not a Target of Opsonic Antibody or Protective Immunity J. Exp. Med., April 30, 2001; 193(9): 1015 - 1026. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. I. Liochev and I. Fridovich Copper- and Zinc-containing Superoxide Dismutase Can Act as a Superoxide Reductase and a Superoxide Oxidase J. Biol. Chem., December 1, 2000; 275(49): 38482 - 38485. [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 |