@article {2447,
	title = {Desulfoferrodoxin: a modular protein},
	journal = {J Biol Inorg Chem},
	volume = {5},
	number = {6},
	year = {2000},
	note = {<p>0949-8257 (Print)0949-8257 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tResearch Support, U.S. Gov{\textquoteright}t, P.H.S.</p>
},
	month = {Dec},
	pages = {720-9},
	abstract = {<p>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(Nepsilon-His)3(Ndelta-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.</p>
},
	keywords = {Amino Acid Sequence, Base Sequence, Cloning, Molecular, Desulfovibrio vulgaris/genetics, DNA Primers, DNA, Bacterial, Ferredoxins/chemistry/*genetics/metabolism, Molecular Sequence Data, Sequence Homology, Amino Acid, Superoxide Dismutase/metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=11128999 },
	author = {Ascenso, C. and Rusnak, F. and Cabrito, I. and Lima, M. J. and Naylor, S. and Moura, I. and Moura, J. J.}
}
