Water is a key factor to alter the structure and electrochemical properties of carboxylate-bridged dimanganese(ii) complexes

Abstract

The synthesis and physical properties of dimanganese(II) compounds with varying numbers of water ligands housed in the four bulky carboxylate motifs, including the first complex with a parallelogram core {Mn2(μ-OH2)2(μ-O2CR)}(3+) unit, are described. The isolation of these complexes revealed how water could alter the structural and electrochemical properties of similar carboxylate-bridged dimanganese(II) cores that may occur in a variety of active sites of Mn-containing metalloenzymes. These studies support the notion that water molecules in coordination spheres of active sites of metalloproteins are not a simple spectator medium but the modulation factor of structures and functions.

Metal Substitution and Solvomorphism in Alkylthiolate-Bridged Zn3 and HgZn2 Metal Clusters

“…The fascinating interplay of structure and function has motivated continuous efforts to prepare synthetic complexes inspired by metalloproteins. Significant advances in our understanding of protein/metal binding sites have come from the investigation of small synthetic complexes. − Although small metal/ligand complexes reproduce only a small fraction of the information encoded within the holoprotein framework, they serve as milestones toward more elaborate models. , …”

“…Multimetallic proteins present especially complex synthetic challenges. ,− The ubiquitous multimetallic metallothionein protein family has a variety of exceptional properties, inviting further study . Unusual structural characteristics of metallothioneins include low homology primary sequences with nearly 30% cysteine residues and tertiary structures varying with metal occupancy.…”