The result of two pieces of work is a field called asymmetric organocatalysis that is now rippling through industrial chemistry
THIS YEAR’S Nobel prize for chemistry was shared by Benjamin List, of the Max Planck Institute for Coal Research, in Germany, and David MacMillan, of Princeton University. Their prize-winning work, published in 2000, was conducted independently, and unknown to each other at the time, but with the same end in mind. This was to break the stranglehold of enzymes and transition metals on the field of catalysis.
Transition metals are those found in the middle of the periodic table, such as copper, nickel and iron. The structures of their electron shells are complicated, meaning they are chemically versatile, which is what makes them good catalysts. Some transition-metal catalysts are the metals themselves. More often, they are small molecules that include a transition-metal atom. Transition-metal catalysts can be easier to handle than enzymes, but usually fail to distinguish between enantiomers.
Dr List worked on an enzyme called aldolase A, which catalyses what is known as the aldol reaction, an important way of forging molecular bonds between carbon atoms. Aldolase A is made of 350 amino acids, the building blocks of proteins, but the bit that does the work consists of only three of these: lysine, glutamic acid and tyrosine. The rest of the enzyme is, essentially, packaging. He therefore wondered if he could isolate the enzyme’s active centre and yet preserve its activity.
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