ABSTRACT
Selective dephosphorylation is full of great challenges in the field of biomimetic catalysis. To mimic the active sites of protein phosphatase, Hf-OH-Hf motif-containing metal-organic frameworks (MOFs) were obtained and structurally characterized, which are assembled from [Hf48Ni6] cubic nanocages and exhibit good stability in various solvents and acid/base solutions. Catalytic investigations suggest as-synthesized Hf-Ni and Hf-Ni-NH 2 display accurate type-selectivity (selectively catalyzed P-O rather than S-O or C-O bonds) and position-selectivity (selectively catalyzed phosphomonoesters over phosphodiesters) for the hydrolysis of phosphoesters. Reaction kinetic studies further revealed the high activity of the catalytic sites in these catalysts, and the unique catalytic selectivity and high activity are comparable to phosphatase. Additionally, these MOF catalysts possess good recursivity and hypotoxicity. Control experiments (including Hf- and Zr-based isomorphous MOFs) and theoretical calculations indicate that both triplet nickel and Hf6 clusters play significant roles in the unique binding site and favorable binding energy. To our knowledge, this is the first example of selective dephosphorylation through MOF catalysts as mimic enzymes, which paves a potential way for the development of specific therapeutic MOFs.
ABSTRACT
RNA cleavage via internal transesterification is a fundamental reaction involved in RNA processing and metabolism, and the regulation thereof. Herein, the influence of ribose conformation on this reaction was investigated with conformationally constrained ribonucleotides. RNA cleavage rates were found to decrease in the order South-constrained ribonucleotide > native ribonucleotide â« North-constrained counterpart, indicating that the ribose conformation plays an important role in modulating RNA cleavage via internal transesterification.
