Interaction of Cyanide with Enzymes Containing Vanadium, Manganese, Non-Heme Iron, and Zinc
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Since the early discovery of Prussian Blue, cyano transition metal complexes have played a fundamental role in coordination chemistry. They represent important compounds with fascinating chemical and physical properties which turn them into valuable tools for both chemists and biologists. HCN as a precursor in prebiotic chemistry has gained interest in view of its polymers being involved in the formation of amino acids, purines, and orotic acid, a biosynthetic precursor of uracil. Clearly, the rapid formation of adenine by aqueous polymerization of HCN is one of the key discoveries in these experiments. They cyanide anion is usually toxic for most aerobic organisms because of its inhibitory effects on respiratory enzymes, but as a substrate it is an important source of carbon and nitrogen for microorganisms, fungi and plants. Most interesingly, the cyanide anion is a ligand of important metal-dependent biomolecules, such as the hydrogenases and the cobalt site in vitamin B12.
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SOSA-TORRES, Martha E., Peter M. H. KRONECK, 2009. Interaction of Cyanide with Enzymes Containing Vanadium, Manganese, Non-Heme Iron, and Zinc. In: SIGEL, Astrid, ed. and others. Metal-carbon bonds in enzymes and cofactors. Cambridge: RSC Publ., 2009, pp. 363-393. Metal Ions in Life Sciences. 6BibTex
@incollection{SosaTorres2009Inter-1132, year={2009}, title={Interaction of Cyanide with Enzymes Containing Vanadium, Manganese, Non-Heme Iron, and Zinc}, number={6}, publisher={RSC Publ.}, address={Cambridge}, series={Metal Ions in Life Sciences}, booktitle={Metal-carbon bonds in enzymes and cofactors}, pages={363--393}, editor={Sigel, Astrid}, author={Sosa-Torres, Martha E. and Kroneck, Peter M. H.} }
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