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Papers In Press, published online ahead of print June 26, 2000
Biochemistry and Molecular Biology and the Section of Hematology Research, Mayo Clinic, Rochester, MN 55905
Corresponding Author: rusnak{at}mayo.edu
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 ortholog (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 anti-oxidant properties of recombinant T. pallidum neelaredoxin. Neelaredoxin was shown to be expressed in T. pallidum by RT-PCR and Western blot analysis. Recombinant neelaredoxin is a 26 kDa a2 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 addition of K3[Fe(CN)6], exhibits an optical spectrum with absorbances at 280, 320, and 656 nm; the latter 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.
J. Biol. Chem, 10.1074/jbc.M003314200
Submitted on April 18, 2000
Revised on June 20, 2000
Accepted on June 26, 2000
Neelaredoxin, an iron-binding protein from the syphilis spirochete, treponema pallidum, is a superoxide reductase
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