Biomimetic asymmetric catalysis

Enzymes are the core for biological transformations in nature. Their structures and functions have drawn enormous attention from biologists as well as chemists since last century. The large demand of bioactive molecules and the pursuit of efficiency and greenness of synthesis have spurred the rapid development of biomimetic chemistry in the past several decades. Biomimetic asymmetric catalysis, mimicking the structures and functions of enzymes, has been recognized as one of the most promising synthetic strategies for the synthesis of valuable chiral compounds. This review summarizes the evolution of asymmetric catalysis inspired by aldolases, vitamin B₁/B₆-dependent enzymes, NAD(P)H, flavin, hydrogenases, heme oxygenases, non-heme oxygenases, and dinuclear/multinuclear metalloenzymes in aspects of biomimetic design, catalyst development and related catalytic transformations. Those well-established synthetic approaches originating from biological reactions have demonstrated the unique prowess of biomimetic asymmetric catalysis in bridging the gap between bio-catalysis and chemical synthesis. [Figure not available: see fulltext.].