STUDIES ON THE MECHANISM OF HYDROGEN TRANSPORT IN ANIMAL TISSUES : VI. INHIBITOR STUDIES WITH SUCCINIC DEHYDROGENASE.

1. The mechanism of succinic dehydrogenase action was studied by means of inhibitors. 2. The enzyme is inhibited by a large number of diverse compounds whose only common denominator appears to be their ability to react with SH groups. These compounds include quinonoid structures, sulfhydryl reagents, sulfhydryl compounds, copper, zinc, selenite, and arsenite. 3. In contrast to the above inhibitors, the action of malonate does not appear to involve sulfhydryl groups and is explained on the basis of its affinity for the enzyme groups which react with the carboxyl groups of succinate. 4. The action of malonate and the sulfhydryl reactants is mutually exclusive, and this fact suggests the conclusion that the sulfhydryl group of the enzyme is located between the carboxyl affinity points. 5. On the basis of the deduced structure of the succinate-activating center of the enzyme, it is suggested that the enzyme may function by oscillating between the EnSH and EnS. forms, rather than by a thiol-disulfide equilibrium.