Iron‐Catalyzed CH Bond Hydroxylation

Abstract Although Nature is using various metalloenzymes to functionalize CH bonds in ambient conditions, functionalization has always remained a challenge in synthetic chemistry. The most studied iron‐containing metalloenzymes are responsible to activate the CH bonds via high valent metal oxo species. Recognizing the ability of the natural metalloenzymes in unactivated CH bond activation scientists have indulged themselves in replicating the natural enzymatic process in laboratory. After decades of intense research, landmark discoveries have been achieved for mimicking both heme and non‐heme‐based iron‐containing catalyst system. In the early 2000s, simple Fe coordination complex [Fe(TPA)(CH 3 CN) 2 ] emerged to be an effective model which can mimic the chemistry of nonheme oxygenases and catalyze a series of organic substrates. In the following years, the mechanistic framework studied for the system has provoked the thought of the development of a series of iron‐containing oxidation catalysts to perform selective functionalization of various organic substrates at ambient temperature and pressure. In this article, we will be discussing the evolution of iron‐based oxidation catalysts by highlighting the key design principles that enable the tuning of their reactivity and selectivity in the oxidation of CH bonds.