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TITLE: On the relative contribution of ionic interactions over iron-sulfur clusters to ferredoxin stability  Full Text
AUTHORS: Sonia S Leal; Claudio M Gomes;
PUBLISHED: 2008, SOURCE: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, VOLUME: 1784, ISSUE: 11
INDEXED IN: Scopus WOS CrossRef
IN MY: ORCID
22
TITLE: Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn2+-containing ferredoxin  Full Text
AUTHORS: Carlos Frazao ; David Aragao; Ricardo Coelho; Sonia S Leal; Claudio M Gomes; Miguel Teixeira ; Maria Armenia Carrondo ;
PUBLISHED: 2008, SOURCE: FEBS LETTERS, VOLUME: 582, ISSUE: 5
INDEXED IN: Scopus WOS
IN MY: ORCID
25
TITLE: Lactoperoxidase folding and catalysis relies on the stabilization of the alpha-helix rich core domain: A thermal unfolding study  Full Text
AUTHORS: Barbara Boscolo; Sonia S Leal; Elena M Ghibaudi; Claudio M Gomes;
PUBLISHED: 2007, SOURCE: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, VOLUME: 1774, ISSUE: 9
INDEXED IN: Scopus WOS CrossRef
IN MY: ORCID
26
TITLE: Studies of the molten globule state of ferredoxin: Structural characterization and implications on protein folding and iron-sulfur center assembly  Full Text
AUTHORS: Sonia S Leal; Claudio M Gomes;
PUBLISHED: 2007, SOURCE: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, VOLUME: 68, ISSUE: 3
INDEXED IN: Scopus WOS CrossRef
IN MY: ORCID
28
TITLE: Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins  Full Text
AUTHORS: Leal, SS; Gomes, CM;
PUBLISHED: 2005, SOURCE: BIOLOGICAL CHEMISTRY, VOLUME: 386, ISSUE: 12
INDEXED IN: Scopus WOS CrossRef
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30
TITLE: The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre
AUTHORS: Urich, T; Bandeiras, TM ; Leal, SS; Rachel, R; Albrecht, T; Zimmermann, P; Scholz, C; Teixeira, M ; Gomes, CM; Kletzin, A;
PUBLISHED: 2004, SOURCE: BIOCHEMICAL JOURNAL, VOLUME: 381, ISSUE: 1
INDEXED IN: Scopus WOS
IN MY: ORCID
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