Sivanesan, Dharmalingam Kannan, Sethuraman Thangadurai, Thangaian Daniel Jung, Kwang-Deog Yoon, Sungho 2024-01-20T09:03:31Z 2024-01-20T09:03:31Z 2021-09-02 2014-08-14 1477-9226 https://pubs.kist.re.kr/handle/201004/126467 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 {Mn-2(mu-OH2)(2)(mu-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. English ROYAL SOC CHEMISTRY NONHEME DIIRON ENZYMES FUNCTIONAL MODELS RIBONUCLEOTIDE REDUCTASE MANGANESE CATALASE ACTIVE-SITES LACTOBACILLUS-PLANTARUM BENZOATE LIGAND CENTERS POTENTIALS ARGINASE Water is a key factor to alter the structure and electrochemical properties of carboxylate-bridged dimanganese(II) complexes Article 10.1039/c4dt00520a 1 DALTON TRANSACTIONS, v.43, no.30, pp.11465 - 11469 DALTON TRANSACTIONS 43 30 11465 11469 scie scopus 000339538300005 2-s2.0-84904107230 Chemistry, Inorganic & Nuclear Chemistry Article NONHEME DIIRON ENZYMES FUNCTIONAL MODELS RIBONUCLEOTIDE REDUCTASE MANGANESE CATALASE ACTIVE-SITES LACTOBACILLUS-PLANTARUM BENZOATE LIGAND CENTERS POTENTIALS ARGINASE Water splitting electrochemical properties Mn complex