Specific RNA dinucleotide cleavage by a synthetic calix[4]arene-based trinuclear metallo(II)-phosphodiesterase

P. Molenveld; Johannes F.J. Engbersen; David Reinhoudt

doi:10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X

Specific RNA dinucleotide cleavage by a synthetic calix[4]arene-based trinuclear metallo(II)-phosphodiesterase

P. Molenveld, Johannes F.J. Engbersen, David Reinhoudt

Faculty of Science and Technology

Research output: Contribution to journal › Article › Academic › peer-review

106 Citations (Scopus)

Abstract

Large rate enhancements and considerable nucleobase specificity in the catalytic transesterification of RNA dinucleotides are observed with the calix[4]arene 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.

Original language	Undefined
Pages (from-to)	3189-3192
Journal	Angewandte Chemie (international edition)
Volume	38
Issue number	38
DOIs	https://doi.org/10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X
Publication status	Published - 1999

Keywords

METIS-106257
IR-11627

Cite this

Molenveld, P., Engbersen, J. F. J., & Reinhoudt, D. (1999). Specific RNA dinucleotide cleavage by a synthetic calix[4]arene-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

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AU - Reinhoudt, David

PY - 1999

Y1 - 1999

N2 - Large rate enhancements and considerable nucleobase specificity in the catalytic transesterification of RNA dinucleotides are observed with the calix[4]arene 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.

AB - Large rate enhancements and considerable nucleobase specificity in the catalytic transesterification of RNA dinucleotides are observed with the calix[4]arene 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.

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KW - IR-11627

U2 - 10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X

DO - 10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X

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Access to Document

10.1002/(SICI)1521-3773(19991102)38:21<3189::AID-ANIE3189>3.0.CO;2-X