Synthesis and reactivity studies of model complexes for dinuclear active sites in metalloenzymes

Summary, in English

Several new polydentate and potentially dinucleating ligands have been synthesized in order to model the coordination environments of a number of structurally related dinuclear active sites in metalloenzymes, including methane monooxygenase, the ribonucleotide reductase R2 protein, urease, arginase, red kidney bean purple acid phosphatase and zinc phosphotriesterase.~ Ligands 1 and 2 have proven to be versatilebuilding blocks for the preparation ofhomodinuclear Fe2, Mn2 and Ni2 complexes which funcion as adequate structural models for hydrolytic enzymes. Stepwise syntheses of heterodinuclear Fe-Zn complexes have been achieved using ligand 2. Reactivity studies indicate that some of these model complexes exhibit biomimetic activity. The catalytic mechanisms of some hydrolytic enzymes, e.g. urease and kidney bean purple acid phosphatase, have been probed using a combination of synthetic and computational modelling approaches.

• Author: Håkan Carlsson; Vladimir Trukhan; Albert Shteinman; Ebbe Nordlander
• Department/s: Department of Chemistry; Chemical Physics
• Publishing year: 2001
• Language: Swedish
• Links: http://dx.doi.org/10.1016/S0162-0134(01)00254-9
• Document type: Poster
• Topic: Inorganic Chemistry
• Status: Published