Design of Multivariate Biological Metal-Organic Frameworks: Toward Mimicking Active Sites of Enzymes.

Abstract

Mimicking enzymatic processes carried out by natural enzymes, which are highly efficient biocatalysts with key roles in living organisms, attracts much interest but constitutes a synthetic challenge. Biological metal-organic frameworks (bioMOFs) are potential candidates to be enzyme catalysis mimics, as they offer the possibility to combine biometals and biomolecules into open-framework porous structures capable of simulating the catalytic pockets of enzymes. In this work, we first study the catalase activity of a previously reported bioMOF, derived from the amino acid L-serine, with formula {CaIICuII6[(S,S)-serimox]3(OH)2(H2O)} · 39H2O (1) (serimox = bis[(S)-serine]oxalyl diamide), which is indeed capable to mimic catalase enzymes, in charge of preventing cell oxidative damage by decomposing, efficiently, hydrogen peroxide to water and oxygen (2H2O2 → 2 H2O + O2). With these results in hand, we then prepared a new multivariate bioMOF (MTV-bioMOF) that combines two different types of bioligands derived from L-serine and L-histidine amino acids with formula CaIICuII6[(S,S)-serimox]2[(S,S)-hismox]1(OH)2(H2O)}·27H2O (2) (hismox = bis[(S)-histidine]oxalyl diamide ligand). MTV-bioMOF 2 outperforms 1 degrading hydrogen peroxide, confirming the importance of the amino acid residue from the histidine amino acid acting as a nucleophile in the catalase degradation mechanism. Despite displaying a more modest catalytic behavior than other reported MOF composites, in which the catalase enzyme is immobilized inside the MOF, this work represents the first example of a MOF in which an attempt is made to replicate the active center of the catalase enzyme with its constituent elements and is capable of moderate catalytic activity.