Sulphydryl groups and enzymic oxido-reduction

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Abstract
The enzyme which catalysed the oxidation of triosephos-phate by pyruvate depended, for its activity, on its state of oxidation-reduction. When oxidized by I2 or by oxidized glutathione (GSSG) its activity was greatly diminished. Such an inactivated enzyme was considerably reactivated on re-reduction by cysteine, GSH, or H2S. The activity of the enzyme was almost totally suppressed on treatment with Cu2O, and almost fully recovered on regenerating the enzyme by H2S. Using coenzyme-free preparations it was shown that the action of Cu2O, oxidants and reductants was mainly concerned with active groups of the enzyme itself. The tentative hypothesis was suggested that these changes in activity of the enzyme under the influence of oxidants and reductants were to be ascribed mainly to the oxidation and reduction of the SH groups of the enzyme.

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