Abstract
In search for peptidic [FeFe] hydrogenase mimics, the cyclic disulfide Sandostatin (octreotide) was allowed to react with Fe(3)(CO)(12). An octreotide-Fe(2)(CO)(6) complex was isolated and characterized spectroscopically as well as by elemental and thermochemical analysis. The complex catalyzes the electrochemical reduction of H(+) to H(2). It is suggested by radioligand binding assays that the complex retains much of the binding affinity for the somatostatin hsst(1-5) receptors of octreotide.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antineoplastic Agents, Hormonal / chemistry*
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Bacterial Proteins / chemistry
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Carbonates / chemistry*
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Catalytic Domain
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Electrochemical Techniques
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Ferric Compounds / chemistry*
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Humans
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Hydrogenase / chemistry
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Iron-Sulfur Proteins / chemistry
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Molecular Structure
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Octreotide / chemistry*
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Somatostatin / chemistry
Substances
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Antineoplastic Agents, Hormonal
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Bacterial Proteins
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Carbonates
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Ferric Compounds
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Iron-Sulfur Proteins
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Somatostatin
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iron hydrogenase
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Hydrogenase
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Octreotide