Towards mimicking metalloenzymes
Oxidised diiron species are used in nature in the active sites of several metalloenzymes, such as methane monooxygenase and ribonucleotide reductase.
Methane monooxygenase catalyses the selective oxidation of methane to methanol and understanding these reaction mechanisms is important in order to develop low-cost methane-to-methanol conversion.
Thorsten Glaser and colleagues from the University of Bielefeld, collaborators from the Max-Planck-Institute for Radiation Chemistry, Mülheim, and co-workers at the Stanford Synchrotron Radiation Laboratory, in California, have oxidised a diferric Fe(III) complex to two Fe(III) radical species. Following decay of these complexes, the identification of a highly reactive Fe(IV) complex ([LFe(IV)=O]) was achieved.
Significantly, the discovery of this Fe(IV) species opens up new pathways to highly oxidised dinuclear complexes which could be applied to biomimetic C-H activation reactions.
‘The future challenges are the enlargement of complexes with more advanced ligands mimicking the second coordination sphere of the enzymes active sites,’ says Glaser.
Studies are already underway in the group, to improve ligand design and stabilise a real dinuclear Fe(IV) complex with reactivities analogous to methane monooxygenase.
Original article: Glaser et. al., Chem. Commun., 2009
Other news from the department science
Get the analytics and lab tech industry in your inbox
From now on, don't miss a thing: Our newsletter for analytics and lab technology brings you up to date every Tuesday. The latest industry news, product highlights and innovations - compact and easy to understand in your inbox. Researched by us so you don't have to.