Desulfoferrodoxin: A modular protein

Carla Ascenso, Frank Rusnak, Inês Cabrito, Maria J. Lima, Stephen Naylor, Isabel Moura, José J. G. Moura

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33 Citations (Scopus)


The gene encoding the non-heme iron-containing desulfoferrodoxin from Desulfovibrio vulgaris was cloned in two fragments in order to obtain polypeptides corresponding to the N- and C-terminal domains observed in the tertiary structure. These fragments were expressed in Escherichia coli, purified to homogeneity and biochemically and spectroscopically characterized. Both recombinant fragments behaved as independent metal-binding domains. The N-terminal fragment exhibited properties similar to desulforedoxin, as expected by the presence of a Fe(S-Cys)4 metal binding motif. The C-terminal fragment, which accommodates a Fe(N(ε)-His)3(N(δ)-His)(S-Cys) center, was shown to have properties similar to neelaredoxin, except for the reaction with superoxide. The activities of desulfoferrodoxin and of the expressed C-terminal fragment were tested with superoxide in the presence and absence of cytochrome c. The results are consistent with superoxide reductase activity and a possible explanation for the low superoxide consumption in the superoxide dismutase activity assays is proposed.

Original languageEnglish
Pages (from-to)720-729
Number of pages10
JournalJBIC Journal of Biological Inorganic Chemistry
Issue number6
Publication statusPublished - 30 Nov 2000


  • Desulfoferrodoxin
  • Desulforedoxin
  • Neelaredoxin
  • Rubredoxin
  • Superoxide oxidoreductase


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