Functional models of non-heme diiron enzymes

✍ Scribed by M. Fontecave; S. Ménage; C. Duboc-Toia

• Book ID: 104111810
• Publisher: Elsevier Science
• Year: 1998
• Tongue: English
• Weight: 379 KB
• Volume: 178-180
• Category: Article
• ISSN: 0010-8545
• DOI: 10.1016/s0010-8545(98)00119-2

✦ Synopsis

Diiron complexes are structural models of active centers of a variety of enzymes (methane monooxygenase, ribonucleotide reductase and purple acid phosphatase). More recently, they proved to have the potential to catalyze the oxidation of alkanes, alcohols, sulfides by peroxides or molecular oxygen (in the presence of electrons) and the hydrolysis of phosphodiesters. By selection of appropriate ligands, some reactions can be made highly selective, as shown from our report of the first enantioselective oxidation catalyzed by a chiral m-oxo diiron complex.