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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/1662

Título: Spectroscopic characterization of a novel 2 /[4Fe /4S] ferredoxin isolated from Desulfovibrio desulfuricans ATCC 27774
Autor: Moura, José J. G.
Rodrigues, Pedro M.
Moura, Isabel
Macedo, Anjos L.
Palavras-chave: Iron /sulfur cluster
2 /[4Fe /4S] clusters
Ferredoxin
Metalloprotein
Paramagnetic protein
Nuclear magnetic resonance
Desulfovibrio desulfuricans ATCC 27774
Issue Date: 2003
Editora: Elsevier B. V.
Resumo: A novel iron /sulfur containing protein, a ferredoxin (Fd), was purified to homogeneity from the extract of Desulfovibrio desulfuricans American type culture collection (ATCC) 27774. The purified protein is a 13.4 kDa homodimer with a polypeptide chain of 60 amino acids residues, containing eight cysteines that coordinate two [4Fe /4S] clusters. The protein is shown to be air sensitive and cluster conversions take place. We structurally characterize a redox state that contains two [4Fe /4S] cores. 1D and 2D 1H NMR studies are reported on form containing the clusters in the oxidized state. Based on the nuclear Overhauser effect (NOE), relaxation measurements and comparison of the present data with the available spectra of the analogous 8Fe Fds, the cluster ligands were specifically assigned to the eight-cysteinyl residues
Descrição: Inorganica Chimica Acta 356 (2003) 215-221
URI: http://hdl.handle.net/10362/1662
ISSN: 0020-1693
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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