Peptide-metal interaction

Carboxypeptidase A was the first zinc enzyme to yield a three-dimensional structure to the X-ray crystallographic method, and the structure of an enzyme-pseudosubstrate complex provided a model for a precatalytic zinc-carbonyl interaction (Lipscomb etai, 1968). Comparative studies have been performed between carboxypeptidase A and thermolysin based on the results of X-ray crystallographic experiments (Argosetai, 1978 Kesterand Matthews, 1977 Monzingoand Matthews, 1984 Matthews, 1988 Christianson and Lipscomb, 1988b). Models of peptide-metal interaction have recently been utilized in studies of metal ion participation in hydrolysis (see e.g., Schepartz and Breslow, 1987). In these examples a dipole-ion interaction is achieved by virtue of a chelate interaction involving the labile carbonyl and some other Lewis base (e.g.. 

Hart BR, Shea KJ. Synthetic peptide receptors molecularly imprinted polymers for the recognition of peptides using peptide-metal interactions. J Am Chem Soc 2001 123 2072-2073. 

Based in part on the article Peptide-Metal Interactions by Justin K. Moran Claude F. Meares which appeared in the Encyclopedia of Inorganic Chemistry, First Edition. 

Nucleic Acid Metal Ion Interactions Nutritional Aspects of Metals Trace Elements Peptide-Metal Interactions Zinc Enzymes Zinc Inorganic Coordination Chemistry. 

Cobalt Inorganic Coordination Chemistry Copper Inorganic Coordination Chemistry Copper Proteins Oxidases Copper Proteins with Dinuclear Active Sites Copper Proteins with Type 2 Sites Cytochrome Oxidase Iron Heme Proteins, Peroxidases, Catalases Catalase-peroxidases Iron Proteins with Mononuclear Active Sites Metal Ion Toxicity Metal-related Diseases of Genetic Origin Metallocenter Biosynthesis Assembly Metalloregulation Peptide Metal Interactions Zinc Enzymes. 

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