Desulfovibrio gigas nlr protein
an iron-binding protein with superoxide reductase activity
Also Known As:
nlr protein, Desulfovibrio gigas; neelaredoxin
Networked: 2
relevant articles (0 outcomes,
0 trials/studies)
Bio-Agent Context: Research Results
Experts
| 1. | Auchère, Françoise:
1 article
(10/2004)
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| 2. | Cordas, Cristina:
1 article
(10/2004)
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| 3. | Moura, Isabel:
1 article
(10/2004)
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| 4. | Moura, José J G:
1 article
(10/2004)
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| 5. | Raleiras, Patricia:
1 article
(10/2004)
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| 6. | Sikkink, Robert:
1 article
(10/2004)
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| 7. | Tavares, Pedro:
1 article
(10/2004)
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| 8. | Ascenso, C:
1 article
(09/2000)
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| 9. | Benson, L M:
1 article
(09/2000)
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| 10. | Hazlett, K R:
1 article
(09/2000)
|
Related Diseases
| 1. | Syphilis
09/15/2000
- " Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase." 10/01/2004
- " Treponema pallidum (Tp), the syphilis spirochete, expresses the gene for a superoxide reductase called neelaredoxin, having the iron protein rubredoxin as the putative electron donor necessary to complete the catalytic cycle. " 09/15/2000
- " 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. "
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