Abstract
The kinetics of penicillin inactivation by various mercaptoamines have been followed by polarimetry. In the case of primary mereaptoamines the reactions are of second order with respect to time and concentration of the reactants. By determining the appropriate rate constants under different conditions of pH and ionic strength the conclusion is reached that the rate limiting step is a bimolecular reaction involving the mercaptide ion. The mechanism probably involves the formation of a semimercaptol. Several possible mechanisms for the role of the amino group in the opening of the β-lactam ring are discussed. The inactivation of penicillin by the tertiary mercaptoamine N:N-dimethylcysteamine nearly follows first order kinetics and gives as end product a partially racemized penicilloic acid.
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