May 20, 1924–July 29, 1988


MYRON LEE BENDER played a major role in bringing enzymology within the compass of chemistry and made outstanding contributions to our understanding of reaction mechanisms in organic chemistry and enzymology. In particular, he and his coworkers unscrambled the kinetics of the action of the serine proteases. They showed how to reconcile the rate data with a two-step mechanism for the hydrolytic process, wherein an enzyme molecule is acylated as it cleaves a peptide bond, and subsequently is regenerated when the acylated enzyme is hydrolyzed. Since the proteases constitute one of the leading systems in the study of enzymes at a molecular level, Bender's research was of great importance to the development of bio-organic chemistry.

While this body of work probably constitutes the most important of Bender's achievements, his earlier contribution to the detailed mechanism of the hydrolysis of esters would alone be sufficient to provide his work with lasting distinction.

Later, he and Koshland working independently invented a chemical procedure to convert the single serine residue in the protease subtilisin to a cysteine and thereby tested the importance of that single change in enzyme structure

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