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

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Abstract
Mercurials selectively inhibited E. coli 414 ATPase (EC 3.6.1.3). Inhibition of the soluble ATPase (BF1) was greater than for the membrane-bound enzyme. The titration of 4 SH groups/mol BF1 with 0.05 mM-p-chloromercuri[14C]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. coli ATPase by inducing a molecular change in the holoenzyme, followed by dissociation. One to 2 SH groups with different degrees of accessibility were located in the .alpha. and .gamma. subunits of ATPase (BF1) but only 1 was located in the .beta. subunit, irrespective of the concentration of p-chloromercuribenzoic acid, suggesting a structural role for SH groups in BF1.

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