Abstract
Monooxygenases are not only some of the most versatile machineries in our lives, but
also some of the most explored enzymes in modern organic synthesis. They provide knowledge
and inspiration on how the most abandoned oxidant, dioxygen, can be activated and
utilized to deliver selective oxidations. This review presents an outline in the mechanisms
that Nature uses to succeed in these processes and recent indicative examples on how
chemists use this knowledge to develop selective oxidation protocols based on dioxygen
as the terminal oxidant.
1 Introduction
2 Monooxygenases
2.1 Metal-Based Monooxygenases
2.1.1 Cytochromes
2.1.2 Copper-Dependent Monooxygenases
2.1.3 Heme-Independent Iron Monooxygenases
2.1.4 Pterin-Dependent Monooxygenases
2.2 Metal-Free Monooxygenases
2.2.1 Flavin-Dependent Monooxygenases
2.2.2 Systems without Cofactors
3 Biomimetic Aerobic Oxidations
3.1 Aerobic Oxidations Based on Metal Catalysts
3.1.1 Epoxidations and Allylic Oxidations
3.1.2 Oxidations of Unactivated Carbon Atoms and Benzylic Oxidations
3.1.3 Oxidations of Aryl Groups
3.1.4 Heteroatom Oxidations
3.2 Aerobic Oxidations Based on Organocatalysts
3.2.1 Baeyer–Villiger Oxidations
3.2.2 Oxidations of Aryl Groups
3.2.3 Heteroatom Oxidations
4 Conclusion
Key words high-valent metal complexes - flavins - biomimetics - C–H oxidations - sustainable
oxidations - green oxidations
