Artificial dinuclear phosphoesterases.
Many elegant dinuclear transition metal and lanthanide complexes that efficiently hydrolyze phosphate esters including RNA and DNA have been reported recently. In most cases, the dinuclear complexes are much more reactive than the corresponding mononuclear metal complexes. Furthermore, structural and kinetic data indicate that substantial rate acceleration for phosphate diester cleavage is obtained by bridging the dinuclear metal centers with the two phosphoryl oxygens. Interestingly, such bridging structures have recently been implicated in several metalloenzyme catalyzed phosphate hydrolyses.
Department of Chemistry, McGill University, Montreal, Quebec, H3A 2K5, Canada. chin@musica.mcgill.ca
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D002384:Catalysis; D004247:DNA / Q000378:metabolism; D006868:Hydrolysis; D008670:Metals / Q000737:chemistry*; D008674:Metals, Rare Earth / Q000737:chemistry*; D008958:Models, Molecular; D010755:Organophosphates / Q000737:chemistry; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012313:RNA / Q000378:metabolism
D008670:Metals; D008674:Metals, Rare Earth; D010755:Organophosphates; D012313:RNA; D004247:DNA; D010744:Phosphoric Monoester Hydrolases