Synthetic nonheme high-valent iron-oxo complexes structures and oxidative function

There has been a large explosion of information in the field of dioxygen activating nonheme iron enzymes since the last edition of Comprehensive Coordination Chemistry, namely Comprehensive Coordination Chemistry II, was published in late 2003. This development is evidenced by the number of chapters on this topic that appear in this volume. There are two chapters written by Yisong Guo and Wei-chen Chang on nonheme monoiron enzymes (co-substrate-dependent and co-substrate-independent subsets), a chapter by Brian Fox on nonheme diiron enzymes, and a chapter by Ivy Ghosh and Tapan Kanti Paine on functional models for oxygen activating nonheme monoiron enzymes. This chapter serves to complement the four chapters mentioned above by focusing on biomimetic analogs of the high-valent iron-oxo oxidants generated by these enzymes. The biomimetic analogs have been synthesized and characterized only since the turn of the millennium and now altogether consist of over a hundred examples. Crystal structures of sixteen such oxoiron(IV) complexes have been solved and provide an excellent basis for understanding the properties of the Fe^IV]O unit. It has certainly been an exciting and productive time for this area of research. There are also a couple of diiron structures with high-valent Fe–O–Fe units. Efforts by Terrence Collins and Miquel Costas have also opened the door for the synthesis and characterization of Fe^V(O) species that shed some light on what such highly reactive species may look like and what types of oxidative chemistry they may be able to perform. This chapter consists of sections covering synthetic....