Factors Controlling the Reactivity of a Ligninase Model Based on the Association of Potassium Monopersulfate to Manganese and Iron Porphyrin Complexes

Article abstract of DOI:10.1021/jo00282a011

An efficient ligninase model based on the association of potassium monopersulfate to iron and manganese porphyrin in solution or immobilized onto an ion-exchange resin is reported.High catalytic conversion of veratryl alcohol or 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol, a useful model molecule for checking the ability of cleaving C_α-C_β bonds of arylglycerol-β-aryl ether linkages existing in lignin itself, is obtained at room temperature in a single-phase solution (buffered water/acetonitrile, 75/25, v/v) at pH 2-3 for iron porphyrin or at pH 4.5-6.0 for manganese porphyrin.The porphyrin ligand used in the present study is the meso-tetrakis(p-sulfonatophenyl)porphyrin (TPPS).Catalytic activities can be as high as eight cycles per second.