Large rate enhancements and considerable nucleobase specificity in the catalytic transesterification of RNA dinucleotides are observed with the calixarene enzyme mimic 1-Zn3 (the computer-generated model of the complex with GpG is shown). The higher activity toward GpG over ApA (factor of 160) originates from favorable substrate binding and cooperative catalytic action of all three ZnII ions. The heterotrinuclear metallo-phosphoesterase mimic 1-Zn2Cu is even more active.
|Journal||Angewandte Chemie (international edition)|
|Publication status||Published - 1999|
Molenveld, P., Engbersen, J. F. J., & Reinhoudt, D. (1999). Specific RNA dinucleotide cleavage by a synthetic calixarene-based trinuclear metallo(II)-phosphodiesterase. Angewandte Chemie (international edition), 38(38), 3189-3192. https://doi.org/10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X