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Gene Review: 

Dde_3193  -  desulfoferrodoxin

Desulfovibrio alaskensis G20

 
 
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Disease relevance of Dde_3193

  • Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774) [1].
  • Desulfoferrodoxin (Dfx), a small iron protein containing two mononuclear iron centres (designated centre I and II), was shown to complement superoxide dismutase (SOD) deficient mutants of Escherichia coli [Pianzzola, M.J., Soubes M. & Touati, D. (1996) J. Bacteriol. 178, 6736-6742] [2].
 

High impact information on Dde_3193

  • Crystals of the fully oxidized form of desulfoferrodoxin were obtained by vapor diffusion from a solution containing 20% PEG 4000, 0.1 M HEPES buffer, pH 7.5, and 0.2 M CaCl2 [3].
  • Upon reaction of fully oxidized Dfx with the superoxide generating system xanthine/xanthine oxidase, Dfx centres I and II become partially reduced, suggesting that Dfx operates by a redox cycling mechanism, similar to those proposed for other SODs [2].
 

Analytical, diagnostic and therapeutic context of Dde_3193

  • The secondary structure did not disappear, according to far-UV circular dichroism (CD), until 6 M GuHCl was added; this transition was reversible (for incubation times of < 1 h) and independent of dfx concentration [DeltaG(H(2)O) = 50 kJ/mol of monomer] [4].

References

  1. Spectroscopic properties of desulfoferrodoxin from Desulfovibrio desulfuricans (ATCC 27774). Tavares, P., Ravi, N., Moura, J.J., LeGall, J., Huang, Y.H., Crouse, B.R., Johnson, M.K., Huynh, B.H., Moura, I. J. Biol. Chem. (1994) [Pubmed]
  2. The superoxide dismutase activity of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774. Romão, C.V., Liu, M.Y., Le Gall, J., Gomes, C.M., Braga, V., Pacheco, I., Xavier, A.V., Teixeira, M. Eur. J. Biochem. (1999) [Pubmed]
  3. Preliminary crystallographic analysis of the oxidized form of a two mono-nuclear iron centres protein from Desulfovibrio desulfuricans ATCC 27774. Coelho, A.V., Matias, P.M., Carrondo, M.A., Tavares, P., Moura, J.J., Moura, I., Fülop, V., Hajdu, J., Le Gall, J. Protein Sci. (1996) [Pubmed]
  4. Equilibrium unfolding of dimeric desulfoferrodoxin involves a monomeric intermediate: iron cofactors dissociate after polypeptide unfolding. Apiyo, D., Jones, K., Guidry, J., Wittung-Stafshede, P. Biochemistry (2001) [Pubmed]
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