Biomimetic Chemistry and Artificial Enzymes: Catalysis by Design

Breslow, Ronald. “Biomimetic chemistry and artificial enzymes: catalysis by design.” Accounts of Chemical Research 28, no. 3 (1995): 146-153.

The highly effective catalysis by Nature’s enzymes has inspired us,[1-2] and others, to imitate it. We coined the terms “biomimetic chemistry” [3] and “arti-ficial enzyme”[621] to describe this field. Of course the design of new catalysts need not slavishly follow what we can learn from enzymes, but it is a good place to start. Enzymes generally bind their substrates and then use the action of two or more well-placed functional groups to achieve catalysis. This scheme leads to substrate selectivity, reaction selectivity, and stereo-selectivity. Binding can be achieved by metal coordi-nation, ion pairing, Lewis acid—base coordination, or hydrogen bonding in nonaqueous solvents, and by metal or Lewis acid—base coordination or hydrophobic interaction in water solution. In our earliest work we used simple metal coordination to hold a substrate next to catalytic groups,[22] but we have chiefly concen-trated on the use of cyclodextrins (Figure 1) that bind hydrophobic substrates in water solution. Various functional groups can be attached to the cyclodextrins, and the cavity can also be modified .[23] Others have examined hydrophobic macrocycles[24-26] or calix-arenes[21,26] for substrate binding in water.

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