title: Structure-function studies on mutants of adrenal ferredoxin.
abstract: Mutants of the adrenal ferredoxin (adrenodoxin) have been expressed in E. coli in order to improve the understanding of its structure and function. Replacement of the ligands to the /2Fe-2S/ center, C46, C52, C55 and C92, by serine, histidine or aspartic acid lead to apoproteins not incorporating the iron-sulfur cluster, whereas C95S forms a functionally active holoprotein. C-terminal deletions up to amino acid 109 affect the conformation around the iron-sulfur cluster in adrenodoxin and the interaction with CYP11A1 and CYP11B1, but not with adrenodoxin reductase. The presence of P108 is necessary for incorporation of the /2Fe-2S/ cluster and obviously for correct folding of adrenodoxin.
authors.affiliation: Max-Delbrück-Centrum für molekulare Medizin (MDC), Berlin.
authors.forename: H
authors.initials: H
authors.lastname: Uhlmann
authors.forename: R
authors.initials: R
authors.lastname: Bernhardt
mesh_terms: D000325:Adrenodoxin / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli; D007700:Kinetics; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011485:Protein Binding; D011994:Recombinant Proteins / Q000096:biosynthesis; D013329:Structure-Activity Relationship
chemical_list: D011994:Recombinant Proteins; D000325:Adrenodoxin