Ted W. Reid (Author)
Douglas S. Gregory (Editor)
Richard Epand (Editor)
Jonathan Kopel (Editor)
Bulletin for the History of Chemistry
Volume: 47
Pages: 222-230
This article is based upon a lecture that Irwin Wilson (Figure 1) gave for his 75th birthday on September 18, 1996. (His actual date of birth was May 8, 1921.) The lecture covered his early work on how acetylcholinesterase catalyzes the hydrolysis of acetylcholine. This led to his demonstration of the formation of a covalent acetyl-enzyme intermediate in the reaction. It should be noted that this was in the days before it was understood that an enzyme could catalyze a chemical reaction by forming a covalent intermediate. Further studies on the mechanism of acetylcholinesterase in his laboratory at Columbia University in 1956 gave rise to the rational design of Pralidoxime (2-pyridine aldoxime methyl chloride; 2-PAM) as a reactivator of the organophosphate-inhibited enzyme.
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