Neil Warren Boaz

Enzymatic esterification of 1-ferrocenylethanol: An alternate approach to chiral ferrocenyl bis-phosphines

Abstract 1-Ferrocenylethanol was enzymatically esterified with high R -enantioselectivity by the lipase from Pseudomonas fluorescens , indicating that this organometallic compound behaves similarly to organic analogs within the enzyme active site (according to an active site model). Efficient separation of the enantiomers was effected by selective reaction of the ester with dimethylamine followed by simple aqueous acid extraction.

A benzisothiazolone class of potent, selective mechanism-based inhibitors of human leukocyte elastase

Abstract A new type of mechanism-based inhibitor of human leukocyte elastase (HLE) is described that are designed to inhibit HLE by a suicide route to form an inhibitor-enzyme complex by cross linking the enzyme active site. A mechanism of HLE inhibition is proposed and was used to design analogues with improved potency. The structure-activity relationships described in this paper are consistent with the proposed mechanism of HLE inhibition, and led to WIN 62785 ( 12 ), the most potent compound in this series with a K i * = 0.3 nM.

Amine assisted enzymatic esterification of 1,2-diol monotosylates

Abstract The enzymatic esterification of 1,2-diol monotosylates in organic solvent under standard conditions often fails to achieve the desired 50% conversion due to enzyme inactivation by acidic contaminants. The inclusion of an amine affords rapid conversion to 50% and provides enhanced enantioselectivity.

The stereochemistry of solvolysis of an acyclic allylic epoxide

Abstract In contrast to solvolysis of cyclic allylic epoxides, the acid-catalyzed solvolyses of optically pure 1,2-epoxy-3-butene using water or alcohols show a high degree of inversion stereoselectivity.