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Spectroscopic characterization of a novel 2 /[4Fe /4S] ferredoxin isolated from Desulfovibrio desulfuricans ATCC 27774
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Orientador(es)
Resumo(s)
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
Palavras-chave
Iron /sulfur cluster 2 /[4Fe /4S] clusters Ferredoxin Metalloprotein Paramagnetic protein Nuclear magnetic resonance Desulfovibrio desulfuricans ATCC 27774
Contexto Educativo
Citação
Editora
Elsevier B. V.