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

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 {Ca(II)Cu(II)(6)[(S,S)-serimox](3)(OH)(2)(H(2)O)} · 39H(2)O (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 (2H(2)O(2) → 2 H(2)O + O(2)). 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 Ca(II)Cu(II)(6)[(S,S)-serimox](2)[(S,S)-hismox](1)(OH)(2)(H(2)O)}·27H(2)O (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.