The structure of iron-sulfur proteins.
Ferredoxins are a group of iron-sulfur proteins for which a wealth of structural and mutational data have recently become available. Previously unknown structures of ferredoxins which are adapted to halophilic, acidophilic or hyperthermophilic environments and new cysteine patterns for cluster ligation and non-cysteine cluster ligation have been described. Site-directed mutagenesis experiments have given insight into factors that influence the geometry, stability, redox potential, electronic properties and electron-transfer reactivity of iron-sulfur clusters.
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Lehrstuhl für Struktur und Chemie der Biopolymere, Universität Bayreuth, Germany. heinrich.sticht@uni-bayreuth.de
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D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D004252:DNA Mutational Analysis; D005288:Ferredoxins / Q000737:chemistry*; D007501:Iron; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013455:Sulfur
D001426:Bacterial Proteins; D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D010940:Plant Proteins; D011994:Recombinant Proteins; D013455:Sulfur; D007501:Iron