Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands.
Biochem Biophys Res Commun
; 188(3): 1131-8, 1992 Nov 16.
Article
em En
| MEDLINE
| ID: mdl-1332711
ABSTRACT
Expression systems for adrenodoxin into the periplasm and the cytoplasm of E. coli have been developed as a prerequisite for site-directed mutagenesis studies. In both systems the /2Fe-2S/ cluster of the protein was correctly assembled, the cytoplasmic one gives, however, a tenfold higher expression level. To determine which of the five cysteines at positions 46, 52, 55, 92, and 95 coordinate the /2Fe-2S/ center, they have been individually mutated into serines. From these mutants, only C95S forms a functionally active holoprotein. Thus, residues 46, 52, 55, and 92 are the cysteines that coordinate the /2Fe-2S/ cluster in adrenodoxin.
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Base de dados:
MEDLINE
Assunto principal:
Adrenodoxina
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article