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Mercurials selectively inhibited Escherichia coli 414 ATPase (EC 3.6.1 .3). Inhibition of the soluble ATPase (BF,) was greater than for the membrane-bound enzyme. The titration of 4 SH groups per mol BF, with 0.05 m~-p-chloromercuri(~~C)benzoate showed a good dose-response curve for the inhibition of basal ATPase but not for the trypsin-stimulated activity. Accessible SH groups did not seem to be related to the active site of the enzyme. Mercurials appeared to affect E.'coZi ATPase by inducing a molecular change in the holo- enzyme, followed by dissociation. One to two SH groups with different degrees of acces- sibility were located in the a and y subunits of ATPase (BF,) but only one was located in the p subunit, irrespective of the concentration of p-chloromercuribenzoic acid, suggesting a structural role for SH groups in BF,.

Inhibition by Mercurial Reagents and Role of SH Groups of the Adenosine Triphosphatase from Escherichia coli 414 Membranes